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Biomedical subjects

M A Rogers

Publications and source records attributed to M A Rogers.

At least 19 recordsLinked to original sources
PubMed1997

Effects of single nightly injections of growth hormone-releasing hormone (GHRH 1-29) in healthy elderly men.

Age-related reductions in growth hormone (GH) and insulin-like growth factor-I (IGF-I) may contribute to decreased muscle mass and strength in older persons. The relationship of this phenomenon to skeletal muscle bioenergetics has not been reported. We sought to determine whether administration of GH-releasing hormone (GHRH) would sustain increases in GH and IGF-I and improve skeletal muscle function and selected measures of body composition and metabolism. We measured GH secretion, muscle strength, muscle histology, and muscle energy metabolism by phosphorus nuclear magnetic resonance spectroscopy (31P-NMRS), body composition, and endocrine-metabolic functions before and after 6 weeks of treatment. Eleven healthy, ambulatory, non-obese men aged 64 to 76 years with low baseline IGF-I levels were treated at home as outpatients by nightly subcutaneous self-injections of 2 mg GHRH for 6 weeks. We measured GH levels in blood samples obtained every 20 minutes from 8:00 PM to 8:00 AM; AM serum levels of IGF-I, IGF binding protein-3 (IGFBP-3), and GH binding protein (GHBP); muscle strength; muscle histology; the normalized phosphocreatine abundance, PCr/[PCr + Pi], and intracellular pH in forearm muscle by NMRS during both sustained and ramped exercise; body composition by dual-energy x-ray absorptiometry (DEXA); lipid levels; and glucose, insulin, and GH levels during an oral glucose tolerance test (OGTT). GHRH treatment increased mean nocturnal GH release (P < .02), the area under the GH peak ([AUPGH] P < .006), and GH peak amplitude (P < .05), with no change in GH pulse frequency or in levels of IGF-I, IGFBP-3, or GHBP Two of six measures of muscle strength, upright row (P < .02) and shoulder press (P < .04), and a test of muscle endurance, abdominal crunch (P < .03), improved. GHRH treatment did not alter exercise-mediated changes in PCr/[PCr + Pi] or intracellular pH, but decreased or abolished significant relationships between changes in PCr/[PCr + Pi] or pH and indices of muscle strength. GHRH treatment did not change weight, body mass index, waist to hip ratio, DEXA measures of muscle and fat, muscle histology, glucose, insulin, or GH responses to OGTT, or lipids. No significant adverse effects were observed. These data suggest that single nightly doses of GHRH are less effective than multiple daily doses of GHRH in eliciting GH- and/or IGF-I-mediated effects. GHRH treatment may increase muscle strength, and it alters baseline relationships between muscle strength and muscle bioenergetics in a manner consistent with a reduced need for anaerobic metabolism during exercise. Thus, an optimized regimen of GHRH administration might attenuate some of the effects of aging on skeletal muscle function in older persons.

Aged↗
PubMed1997

Mutations in the hair cortex keratin hHb6 cause the inherited hair disease monilethrix.

Pathogenic mutations in a large number of human epithelial keratins have been well characterized. However, analogous mutations in the hard alpha-keratins of hair and nail have not yet been described. Monilethrix is a rare autosomal dominant hair defect with variable expression. Hairs from affected individuals show a beaded structure of alternating elliptical nodes and constrictions (internodes). These internodes exhibit a high prospensity to weathering and fracture. Strong evidence that trichocyte keratin defects might underlie this hair disorder was provided by genetic linkage analyses that mapped this disease to the type-II keratin gene cluster on 12q13. All affected individuals from a four-generation British family with monilethrix, previously linked to the type-II keratin gene cluster, as well as three unrelated single monilethrix patients, exhibited a heterozygous point mutation in the gene for type-II hair cortex keratin hHb6, leading to lysine substitution of a highly conserved glutamic acid residue in the helix termination motif (Glu 410 Lys). In a three-generation French family with monilethrix of a milder and variable phenotype, we detected another heterozygous point mutation in the same glutamic acid codon of hHb6, which resulted in a conservative aspartic acid substitution (Glu 410 Asp). These mutations provide the first direct evidence for involvement of hair keratins in hair disease.

Adolescent↗
PubMed1997

Sequences and differential expression of three novel human type-II hair keratins.

As part of a program designed to characterize human hair keratin genes and their expression, we present the cDNA sequences and deduced amino acid sequences of three type-II hair keratins hHb3, hHb5, and hHb6, which by virtue of their amino acid homologies are the orthologs of the previously described sheep wool keratins, K2.10, K2.12, and K.211 [29]. Amino acid sequences comparisons of these keratins, including the previously characterized human K2.9 ortholog hHb1, show extreme conservation not only in the alpha-helices but also in the aminoterminal and proximal carboxyterminal domains. They also demonstrate higher sequence relationships between hHb1, hHb3, and hHb6 as compared to hHb5, which exhibits chain-specific sequences in both the head and tail domains. In situ hybridization studies using specific 3'-probes for the four type-II hair keratins reveal sequential patterns of gene expression in human anagen follicles. Remarkably the onset of hHb5 mRNA synthesis occurs immediately above a small population of matrix cells at the base of the hair bulb and the trichocytes lining the dermal papilla. hHb5 mRNA synthesis extends upward through the matrix and ends in the lower part of the cortex of the hair shaft. In contrast, both hHb1 and hHb3 mRNA synthesis begins simultaneously in the cortex 10-15 cell layers above the apex of the dermal papilla, thus partially overlapping that of hHb5 but continuing to a point well beyond hHb5 in the upper cortex. Synthesis of hHb6 mRNA starts slightly higher than either hHb1 or hHb3 mRNA and proceeds much farther up into the keratogenous zone of the hair shaft. Our study demonstrates that the differentiation of human hair in terms of hair keratin expression begins much earlier than previously assumed, i.e. in lower matrix cells of the hair bulb. This early phase of hair differentiation is followed by a late cortical phase of terminal differentiation which comprises at least three type-II hair keratins in the zone of elongation and the keratogenous zone of the hair shaft.

Amino Acid Sequence↗
PubMed1997

Effects of exercise training on glucose transport and cell surface GLUT-4 in isolated rat epitrochlearis muscle.

The effects of exercise training on maximal glucose transport activity and cell surface GLUT-4 were examined in rat epitrochlearis muscle. Five days of swim training (2 x 3 h/day) produce a significant increase in citrate synthase activity (24.5 +/- 0.6 vs. 20.1 +/- 0.7 micromol x min(-1) x g(-1)), GLUT-4 content (22.9 +/- 0.8 vs. 17.4 +/- 0.4% GLUT-4 standard), and glycogen levels (54.3 +/- 9.4 vs. 28.6 +/- 9.4 micromol/g). Maximally, insulin-stimulated glucose transport activity and cell surface GLUT-4 are increased by 55 (1.50 +/- 0.11 vs. 0.97 +/- 0.10 micromol x ml(-1) x 20 min(-1)) and 48% [12.0 +/- 0.8 vs. 8.1 +/- 0.9 disintegrations x min(-1) (dpm) x mg(-1)], respectively, in exercise-trained epitrochlearis muscles. In contrast, hypoxia-stimulated glucose transport activity and cell surface GLUT-4 are reduced by 38 (0.78 +/- 0.08 vs.1.25 +/- 0.14 micromol x ml(-1) x 20 min(-1)) and 40% (5.7 +/- 0.9 vs. 9.4 +/- 1.2 dpm/mg), respectively, in exercise-trained epitrochlearis muscles. These results demonstrate that changes in insulin- and hypoxia-stimulated glucose transport activity after exercise training are fully accounted for by the appearance of cell surface GLUT-4 and support the concept of two intracellular pools of GLUT-4. Finally, we propose that high levels of muscle glycogen with exercise training may contribute to the decrease in hypoxia-stimulated glucose transport activity.

Animals↗
PubMed1997

Fibrinolytic responses to acute physical activity in older hypertensive men.

We tested the hypothesis that the fibrinolytic response to acute physical activity is impaired in sedentary older hypertensive men, which may contribute to the risk of exertion-triggered acute myocardial infarction in this population. Tissue-type plasminogen activator (t-PA) antigen and activity and plasminogen activator inhibitor-1 (PAI-1) antigen and activity were measured in 12 hypertensive (69 +/- 1 yr) and 11 normotensive (64 +/- 1 yr) men before and after an acute bout of submaximal exercise. Contrary to our hypothesis, there were no differences between the two groups in the fibrinolytic response to exercise. t-PA antigen and activity were significantly elevated in both the hypertensive (38 and 172%, respectively) and normotensive (45 and 130%, respectively) groups immediately after exercise but they returned to resting levels within 30 min. There was no change in PAI-1 antigen levels immediately after exercise in either group; however, PAI-1 antigen was significantly lower at 30 and 60 min postexercise in both the hypertensive (31 and 16%, respectively) and normotensive (35 and 20%, respectively) groups. PAI-1 activity was significantly lower immediately after exercise in both the hypertensive (25%) and normotensive (22%) groups and remained lower than preexercise levels at 30 min (23 and 26%, respectively) and 60 min (16 and 12%, respectively) postexercise in both groups. The results of this study demonstrate that the fibrinolytic response to an acute bout of moderate physical activity is not impaired in sedentary older hypertensive men.

Aged↗
PubMed1996

Effects of chromium and resistive training on muscle strength and body composition.

Sixteen untrained males (23 +/- 4 yr), were studied to determine the effects of chromium (Cr) supplementation (200 micrograms.d-1) and a 12-wk resistive exercise training program on muscle strength, body composition, and Cr excretion. The subjects trained 3 times per week with two sets of 8-10 repetitions at 90% of 1 repetition maximum using Keiser variable resistance machines. Food records were used to estimate Cr intake (approximately 36 micrograms.d-1), energy intake, and the percent kJ from protein. The resistive training program resulted in significant increases in total body muscular strength in both the Cr and placebo groups (24% and 33%; P < 0.05). Body weight, percent body fat, lean body mass, and skinfold thicknesses were unchanged in either group after resistive training. Cr excretion increased in the Cr group after 6 wk of Cr supplementation (0.15 +/- 0.08 vs 1.52 +/- 1.26 micrograms.d-1; P < 0.01) and remained higher at 12 wk of training (2.03 +/- 1.73). These results indicate that Cr supplementation, in conjunction with a progressive, resistive exercise training program, does not promote a significant increase in strength and lean body mass, or a significant decrease in percent body fat. Cr supplementation results in a significant increase in Cr excretion that is not altered by resistive training.

Adult↗
PubMed1996

The region coding for the helix termination motif and the adjacent intron 6 of the human type I hair keratin gene hHa2 contains three natural, closely spaced polymorphic sites.

Mutations in distinct sites of epidermal keratins, in particular in the helix initiation and termination regions, cause human genodermatoses due to faulty intermediate filament formation. Extension of this observation to human hereditary hair and nail diseases includes population analyses of human hair keratin genes for natural sequence variations in the corresponding sites. Here we report on a large-scale genotyping of the short helix termination region (HTR) of the human type I cortical hair keratins hHa1, a3-I, and a3-II, and the cuticular hair keratin hHa2. We describe two polymorphic loci, P1 and P2, exclusively in the cuticular hHa2 gene, both creating dimorphic protein variants. P1 is due to a C to T mutation in a CpG element leading to a threonine to methionine substitution; P2 concerns a serine codon AGT that also occurs as an asparagine coding variant AAC. A third polymorphism, P3, is linked with a C to T point mutation located at the very beginning of intron 6. The three polymorphic sites are clustered in a 39-nucleotide sequence of the hHa2 gene. Both allelic frequency calculations in individuals of different races and pedigree studies indicate that the two-allelic hHa2 variants resulting from P1 and P2 occur ubiquitously in a ratio of about 1:1 (P1) and 2:1 (P2) respectively in our survey, and are clearly inherited as Mendelian traits. A genotype carrying both mutations simultaneously on one allele could not be detected in our sampling, and there was no association of a distinct allelic hHa2 variant with the known ethnic form variations of hairs. Sequence comparisons of the HTR of hHa2 with those of other type I hair keratins including the hHa2-ortholog from chimpanzee provide evidence that the P1- and P2-linked mutations must have occurred very early in human evolution and that the two P2-associated codon variants may be the result of two independent point mutations in an ancestral AGC serine codon. These data describe natural polymorphisms in the HTR of a member of the keratin multigene family.

Alleles↗
PubMed1996

Genomic characterization of the human type I cuticular hair keratin hHa2 and identification of an adjacent novel type I hair keratin gene hHa5.

Hair keratins, a subset of the keratin multigene family expressed in hard keratinizing structures, previously have been thought to comprise four members of each subfamily, designated Ha1-4 (type I) and Hb1-4 (type II), which are differentially expressed in the cuticle and cortex of the hair follicle. This report describes the genomic cloning and sequencing of the human type I cuticular hair keratin hHa2, as well as the identification of a previously unknown human type I hair keratin gene. The 12.5-kilobase pair genomic clone ghkI2.12, obtained by hybridization of a human genomic deoxyribonucleic acid library with a 3'-complementary deoxyribonucleic acid probe of hHa2, as well as the partially overlapping 14.4-kilobase pair genomic clone ghkI2.17, isolated using a 5'-fragment of clone ghkI2.12, allowed the characterization of the entire hHa2 gene. The gene displays the same exon/intron structure as two previously characterized type I mouse and sheep hair/wool keratin genes with strict positional conservation of the six introns in the region coding for the central alpha-helix. At the 5'-extremity of clone ghkI2.17, i.e., approximately 8.0 kilobase pairs upstream of the hHa2 gene and oriented in the same transcriptional direction, lies the gene for a hitherto unknown human type I hair keratin. Clone ghkI2.17 contains partial sequence information for this gene beginning with intron 5 and extending to the end of the gene. Screening of a human scalp complementary deoxyribonucleic acid library with a 3'-fragment of the gene yielded a full length complementary deoxyribonucleic acid clone of the new hair keratin, which in continuation of the current nomenclature for hair keratins was termed hHa5. Remarkably, the hHa5 gene, which contains an additional 7th intron in its 3'-noncoding region, is expressed mainly in supramatricial cells and lowermost cortical cells of the hair bulb and thus constitutes a very early component of hair morphogenesis. Our results confirm the type specific clustering of keratin genes and indicate that the human type I hair keratin subfamily contains more members than previously assumed.

Amino Acid Sequence↗
PubMed1996

The fibrinolytic system is not impaired in older men with hypertension.

The fibrinolytic system is thought to be impaired in older hypertensive adults, thus contributing to the elevated risk of atherothrombosis, stroke, and acute myocardial infarction in this population. However, studies that have examined the fibrinolytic system in hypertensive individuals have failed to control for the confounding effects of other metabolic risk factors, making it difficult for one to determine the independent effect of hypertension on the fibrinolytic system. The purpose of the present study was to test the hypothesis that the fibrinolytic system is not impaired in older sedentary hypertensive men when the confounding effects of cardiovascular disease, diabetes, and dyslipidemia are controlled. Plasma concentrations of tissue-type plasminogen activator antigen and activity as well as plasminogen activator inhibitor-1 antigen and activity were measured under resting conditions in 12 hypertensive (69.4 +/- 1.4 years) and 11 normotensive 65.2 +/- 1.3 years) older men. The hypertensive and normotensive subjects had similar anthropometric and metabolic characteristics. There were no significant differences between the hypertensive and normotensive men in tissue-type plasminogen antigen (7.3 +/- 0.5 versus 6.1 +/- 0.6 ng/mL) and activity (1.8 +/- 0.3 versus 1.7 +/- 0.2 IU/mL) or plasminogen activator inhibitor-1 antigen (14.1 +/- 2.3 versus 10.8 +/- 2.2 ng/mL) and activity (17.4 +/- 1.2 versus 17.5 +/- 1.8 arbitrary units [AU]/mL) levels. In addition, the molar concentration ratio of active tissue type plasminogen activator to active plasminogen activator inhibitor-1 did not differ between the hypertensive (1:9.7 +/- 2.3) mmol/L) and normotensive (1:10.5 +/- 2.2 mmol/L) subjects, indicative of no impairment in fibrinolytic potential in either group. These results support the hypothesis that hypertension does not directly result in impaired fibrinolytic function in older adults. Furthermore, our findings suggest that abnormalities in fibrinolytic function in older hypertensive men are likely due to the primary effects of other metabolic disorders that usually accompany hypertension, such as hyperinsulinemia and dyslipidemia.

Aged↗
PubMed1995

ET-18-OCH3 inhibits nuclear factor-kappa B activation by 12-O-tetradecanoylphorbol-13-acetate but not by tumor necrosis factor-alpha or interleukin 1 alpha.

1-O-Octadecyl-2-O-methyl-rac-glycero-3-phosphocholine (ET-18-OCH3) is a synthetic diether phospholipid that is competitive with phosphatidylserine binding to the regulatory domain of protein kinase C (PKC). Our previous studies indicate that the selective inhibition of tumor cell growth by ET-18-OCH3 may be due to altered signal transduction mechanisms, including the inhibition of PKC. To further define the mechanism of action of ET-18-OCH3, we have used it to study the role of PKC in regulation of the transcription factor NF-kappa B, which is activated by diverse stimuli. In the 293.27.2 human kidney cell line, as in hematopoietic cells of all lineages, NF-kappa B is stimulated by 12-O-tetradecanoylphorbol-13-acetate (TPA), tumor necrosis factor-alpha (TNF-alpha), and interleukin-1 alpha (IL-1 alpha). The response to either TNF-alpha or IL-1 alpha is synergistically enhanced by TPA. However, the regulatory mechanisms and signal transduction systems responsible for NF-kappa B activation in response to these different stimuli have not been determined in detail. We have used ET-18-OCH3 and auranofin, which inhibit PKC by different mechanisms, to assess the role of PKC in NF-kappa B activation. ET-18-OCH3 markedly inhibits TPA-induced NF-kappa B activation, as measured by HIV long terminal repeat-directed expression of beta-galactosidase. The IC50 for inhibition by ET-18-OCH3 is approximately 2 microM, a noncytotoxic concentration. Inhibition of TPA-induced NF-kappa B activation was dependent upon preincubation with ET-18-OCH3, and the drug was active at approximately 2 mol% of total cellular phospholipid. ET-18-OCH3 did not inhibit NF-kappa B activation by either TNF-alpha or IL-1 alpha, indicating that there are multiple distinct signal transduction pathways leading to activation of NF-kappa B. We have confirmed these results using auranofin, an antirheumatic drug that is a specific PKC inhibitor interacting with the catalytic domain. Like ET-18-OCH3, auranofin blocked NF-kappa B activation by TPA but not by TNF-alpha or IL-1 alpha. Also like the ether lipid, auranofin only partially blocked the synergy exhibited by TPA and TNF-alpha. To confirm the role of NF-kappa B in this response, we measured NF-kappa B by electrophoretic mobility shift assay. Both ET-18-OCH3 and auranofin inhibited cellular induction of the active NF-kappa B complex in response to TPA but not in response to TNF-alpha.(ABSTRACT TRUNCATED AT 400 WORDS)

Antineoplastic Agents↗
PubMed1995

A cDNA encoding the human type I hair keratin hHal.

A full-length cDNA of a human type I hair keratin was isolated that encodes a protein of 416 amino acids. Northern blot analysis shows that the mRNA is present in human scalp but not in hairless skin. Based on sequence homology comparisons with the four known mouse type I hair keratins mHal-4 the keratin could be identified as the human hair keratin hHal.

Amino Acid Sequence↗
PubMed1995

Sequence data and chromosomal localization of human type I and type II hair keratin genes.

A cDNA library constructed with poly(A)+ RNA from human scalp was screened with selected fragments of both murine type I and type II hair keratin cDNAs. Two keratin clones, one type I, phKI-2, and one type II, phKII-1, were isolated and sequenced. In Northern blots, cDNA probes containing the 3'-noncoding sequences of the clones specifically hybridized to scalp mRNA species. Based on sequence homology comparisons with the four known murine type I hair keratins mHa1-4, the phKI-2 encoded keratin could be identified as human hair keratin hHa2. Similarly, sequence comparison with the four type II sheep wool keratins K2.9-12 revealed an orthologous relationship between the largest member of the type II wool keratin subfamily, K2.9 (i.e., sHb1) and the phKII-1 encoded human hair keratin (hHb1). The specific 3'-noncoding sequences of hHa2 and hHb1 were also used to isolate genomic fragments for both keratins from human genomic libraries which were than used for fluorescence in situ hybridization to human metaphase chromosomes. The hHa2 gene could be mapped to the long arm of chromosome 17, whereas the hHb1 gene was found on the long arm of chromosome 12. DAPI banding of the chromosomes allowed sublocalization of the hHa2 gene to 17q12-q21 and the hHb1 gene to 12q13, i.e., gene loci that have also been previously determined for human type I and type II epithelial keratins.

Amino Acid Sequence↗
PubMed1995

Effects of strength training on muscle hypertrophy and muscle cell disruption in older men.

To determine whether a total body, heavy resistance, strength training (ST) program can significantly increase muscle strength and hypertrophy without muscle cell disruption and soreness in older men, 35 sedentary male subjects between the ages of 50 and 69 years of age (60 +/- 5, mean +/- SD) were studied. Twelve served as inactive controls. Muscular strength, cross-sectional muscle area, serum creatine kinase (CK) activity and perceived soreness were assessed before and after a 16 wk heavy resistance ST program. The ST program resulted in a 43% increase in muscular strength (p < 0.001), and a 7.2% increase in midthigh muscle area (153 +/- 24 vs 164 +/- 23 cm2, p < 0.001). There were no significant changes in strength or muscle area in the inactive control group. Peak serum CK levels were approximately twofold above baseline (278 +/- 175 vs 133 +/- 88 U/l, p < 0.01) 8 h after the first regular training session. At the end of training, the peak rise in CK levels was also reached 8 h after exercise, but was reduced substantially at the same absolute (p < 0.01) and relative resistance loads (p < 0.01) compared to the first training session. Muscle soreness after exercise was only occasionally reported at the beginning of training and was almost nonexistent after training. These results indicate that middle-aged and older men can safely participate in a total body strength training program, intense enough to produce substantial increases in muscle strength and hypertrophy, without promoting muscle soreness or significant muscle cell disruption.(ABSTRACT TRUNCATED AT 250 WORDS)

Adipose Tissue↗
PubMed1995

Testosterone, growth hormone and IGF-I responses to acute and chronic resistive exercise in men aged 55-70 years.

We investigated the responses of serum testosterone (T) and human growth hormone (hGH) concentrations to a bout of heavy resistive exercise and the responses of T, hGH, and insulin-like growth factor I (IGF-I) to a 16 wk progressive resistive training program in 13 men (60 +/- 4 yrs). Body composition via hydrostatic weighing and muscle strength using a 3 repetition maximum (3RM) test on 6 variable resistance exercise machines were assessed before and after the training program. Fasting blood samples were drawn on 2 consecutive days prior to training and again on 2 consecutive days after the last day of exercise. Blood was also drawn immediately before and approximately 10 min after a single exercise session during the first wk of training, and after an exercise session of the same relative resistance during the last wk of training. The training program resulted in a 37% increase in upper body strength and a 39% increase in lower body strength (both p < 0.01). Lean body mass increased significantly (61.8 +/- 2.1 vs 63.7 +/- 7.8 kg; p < 0.001) while % fat decreased (26.5 +/- 1.5 vs 24.9 +/- 6.0%; p < 0.01) as a result of training. Serum T concentration was unchanged, but GH increased approximately 18-fold in response to a single bout of resistive exercise before (0.24 +/- 0.08 vs 4.60 +/- 1.35 mg/l) and after (0.26 +/- 0.06 vs 4.66 +/- 1.46 mg/l; p < 0.01) training. Baseline serum concentrations of T, hGH, and IGF-I were unaffected by the training program. We conclude that an acute bout of resistive exercise causes a substantial hGH response in older men, but 16 wks of progressive resistive training does not affect baseline concentrations of the anabolic hormones.

Aged↗
PubMed1995

Indicators of poor dietary habits in a high risk population.

OBJECTIVE: This study was conducted to determine whether individuals attending an urban outpatient clinic met the National Health Promotion and Disease Prevention nutritional objectives and to assess factors associated with poor dietary habits. METHODS: Individuals who attended the general medicine outpatient clinic at the State University of New York Health Science Center in Syracuse were interviewed using an expanded version of the Health Habits and History Questionnaire. Usual dietary intake, medical history, occupation, stress, physical activity, tobacco use and other life-style factors were recorded. Of particular interest were the percentage of calories from fat in the diet and whether individuals consumed the daily requirements of the base-foods in the USDA Pyramid (grains, vegetables and fruits). Unconditional logistic regression was used to determine odds ratios (OR) and 95% confidence intervals for variables associated with high fat consumption and low consumption of vegetables, fruit and high-fiber grains. RESULTS: None of the patients met the minimal recommended daily servings for the three base-food categories combined (grains, vegetables and fruits) and 84% of subjects had fat intakes which constituted over 30% of daily energy intake. Individuals with less education, who were disabled or unemployed, and who participated in little physical activity were twice as likely to have poor dietary habits (i.e. low consumption of vegetables, fruit, and/or high-fiber grains) as other subjects (p < 0.05). Younger patients (20-49 years of age), especially those who were nonsmokers and who reported little physical activity were more likely to consume fat and less likely to consume fruit than older patients (> or = 50 years of age). Nonwhite subjects were less likely to consume high-fiber grains and whole-wheat breads than white patients (p = 0.04). CONCLUSIONS: Nutritional screening should be considered for all patients attending similar inner-city general medicine clinics, regardless of the primary diagnosis in order to provide early dietary intervention. In particular, young adults, the unemployed, and the disabled should not be overlooked.

Adult↗
PubMed1994

Estrogen receptor expression of benign breast epithelium and its association with breast cancer.

We conducted a case-control study of estrogen receptor (ER) and progesterone receptor (PgR) expression in benign breast epithelium from 120 women (51 breast cancer cases and 69 benign disease controls) who underwent breast operations at University Hospital, Syracuse, New York. Benign samples were obtained and processed immunohistochemically for ER and PgR (Abbott, Chicago, IL). Receptor positivity was defined as any nuclear immunostaining. Proportionately more cases than controls were ER positive (84% versus 57%); PgR positivity was similar in cases and controls (86%). Logistic regression yielded an adjusted odds ratio of 6.5 for breast cancer among ER-positive women (95% confidence interval of 1.5 and 27.4); odds ratio of PgR positivity was 0.3 (95% confidence interval of 0.1 and 1.9). Adjustment for known risk factors for breast cancer did not change the odds ratio. ER-positive breast epithelium needs evaluation as a possible risk marker for breast cancer.

Adult↗