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Biomedical subjects

K Sanada

Publications and source records attributed to K Sanada.

At least 73 records · Page 4Linked to original sources
PubMed1983

[Salivary peptide P-C (III). Its relation to the pathogenesis of diabetes mellitus].

Previous immunohistochemical study showed that salivary peptide P-C like immunoreactivity, originally isolated from whole human saliva, was present not only in human salivary glands but also in human pancreatic B-cells. To elucidate the pathophysiological role of this peptide-like immunoreactivity in human pancreatic B-cells, immunohistochemical study using antisera against both insulin and peptide P-C was carried out on the paraffin embedded pancreatic tissues of 27 diabetic patients and 30 control subjects. Positive immunofluorescence due to insulin was detected in 96% of the diabetic pancreases and 100% of the controls. A pancreas of only one IDDM did not have any immunofluorescence due to insulin. Thus, no significant differences were seen in connection with the presence of insulin between pancreases of NIDDM and the controls, though the present study did not examine whether the number of pancreatic B-cells in the pancreas of NIDDM was the same as that in the controls or not. In contrast, positive immunofluorescence due to peptide P-C like immunoreactivity was demonstrated in only 41% of the diabetic pancreases but in 87% of the controls. In view of the fact that the diabetic pancreases and the controls were fixed and embedded into paraffin in the same department of pathology and under the same conditions, the negative finding for salivary peptide P-C like immunoreactive in the diabetic pancreas seems to result neither from the effects of fixatives nor the destructive postmortem effects of enzymes on the antigenicity of peptide P-C like immunoreactivity but from the decreased content of peptide P-C like immunoreactivity in the diabetic pancreas.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗
PubMed1983

[The presence of proline-rich peptide P-C like immunoreactivity in the human pancreatic B-cells].

It is well known that there are functional and morphological similarities between the salivary glands and the pancreas. Amylase, kallikrein and glucagon are present in both tissues. Morphological similarities of the two tissues have been observed by using a light and electron microscope. In order to examine the pathophysiological relationship between the pancreas and the salivary glands, an immunohistochemical study using antisera against proline-rich peptide P-C, which was recently isolated from human whole saliva, was carried out on the human salivary glands and the pancreas. Peptide P-C like immunoreactivity was found not only in the salivary glands but also in the pancreatic islets. Furthermore, observation of serial thin sections immunostained with insulin, glucagon, somatostatin, PP antisera and antisera against peptide P-C revealed that peptide P-C like immunoreactivity-containing cells were identical to insulin containing B-cells. As the antisera against peptide P-C did not have any cross-reactivity to other kinds of peptide including insulin, glucagon, somatostatin, pp, VIP, human C-peptide and kallikrein, the present finding suggests that peptide P-C like immunoreactivity is present in the B-cells independently of insulin and proinsulin. The finding seems to be a new addition to the lists of proof which support the presence of a pathophysiological relation between the salivary glands and the pancreas. Although it seems likely that peptide P-C like immunoreactivity in the pancreatic B-cells may play some role in the function of the B-cells, since this material was present only in the B-cells among four kinds of cells in the pancreatic islets, its exact pathophysiological role remains to be elucidated.

Humans↗
PubMed1983

Organic acids and branched-chain amino acids in body fluids before and after multiple exchange transfusions in maple syrup urine disease.

We successfully treated a critically ill infant with the classical type of maple syrup urine disease by multiple exchange transfusions via a peripheral artery and vein and with positive calorie supplementation in the early stage of therapy. Clinical improvement was definite after the plasma leucine level fell below 1 mmol/l. There was a close linear correlation between plasma concentrations of branched-chain amino acids and their corresponding branched-chain alpha-keto acids and branched-chain alpha-hydroxy acids. alpha-Hydroxy acids were more easily excreted in the urine than alpha-keto acids and amino acids. Our studies on urinary organic acids supported the existence of minor metabolic pathways of branched-chain alpha-keto acids, although they were not thought to be important in eliminating accumulated alpha-keto acids. Urinary excretion of succinic acid and alpha-ketoglutaric acid, which are components of the citric acid cycle, increased transiently during the patient's convalescence. The cerebrospinal fluid/plasma ratios for branched-chain amino acids, alpha-keto acids, and alpha-hydroxy acids were very high before the transfusions and decreased after improvement. The cerebrospinal fluid/plasma ratios for 5-carbon acids, alpha-ketoisovaleric acid and alpha-hydroxyisovaleric acid were much higher than for other branched-chain acids not only in the patient but also in normal controls. Cerebrospinal fluid levels of alpha-ketoisocaproic acid and alpha-hydroxyisovaleric acid were as high as 1 mmol/l in our patient.

Amino Acids, Branched-Chain↗
PubMed1983

Amino acid sequences of glycopeptides obtained from basic proline-rich glycoprotein of human parotid saliva.

A proline-rich glycoprotein, in which proline, glutamic acid, and glycine represent about 80 per cent of the total residues, was obtained from human parotid saliva. The amino acid sequences of glycopeptides obtained from digests of the glycoprotein with clostripain were determined to be Pro-Gly-Lys-Pro-Glu-Gly-Pro-Pro-Pro-Gln-Gly-Gly-Asn(CHO)-Gln-Ser-Gln-Gly-Pro- Pro-Pro-Arg and Pro-Pro-Gln-Gly-Gly-Asn(CHO)-Gln-Ser-Gln-Gly-Pro-Pro-Pro-His-Pro-Gly-Lys-Pro -Glu-Arg. The structural relationship between the glycopeptides and the known salivary peptide is discussed.

Amino Acid Sequence↗
PubMed1983

Complete amino acid sequence of a basic proline-rich peptide, P-F, from human parotid saliva.

The complete amino acid sequence of a basic proline-rich peptide, P-F, isolated from human parotid saliva was determined to be Ser-Pro-Pro-Gly-Lys-Pro-Gln-Gly-Pro-Pro-Pro-Gln-Gly-Gly-Asn-Gln-Pro-Gln-Gly-Pro-Pro-Pro-Pro-Pro-Gly-Lys-Pro-Gln-Gly-Pro-Pro-Pro-Gln-Gly-Asn-Lys-Pro-Gln-Gly-Pro-Pro-Pro-Pro-Gly-Lys-Pro-Gln-Gly-Pro-Pro-Pro-Gln-Gly-Ser-Lys-Ser-Arg-Ser-Ala by conventional methods. P-F contains a number of repeating sequences and oligo-proline structures identical with those in other proline-rich peptides such as P-C, P-D, P-E, and Protein C. P-F has the highest degree of homology with P-E among these proline-rich peptides.

Amino Acid Sequence↗
PubMed1983

Further fractionation of basic proline-rich peptides from human parotid saliva and complete amino acid sequence of basic proline-rich peptide P-H.

Three basic proline-rich peptides were newly isolated from human parotid saliva, and designated as P-G, P-H, and P-I. The amino acid sequence of P-H was determined to be Ser-Pro-Pro-Gly-Lys-Pro-Gln-Gly-Pro-Pro-Gln-Gln-Glu-Gly-Asn-Asn- Pro-Gln-Gly-Pro-Pro-Pro-Pro-Ala-Gly-Gly-Asn-Pro-Gln-Gln-Pro-Gln-Ala-Pro-Pro- Ala-Gly-Gln-Pro-Gln-Gly-Pro-Pro-Arg-Pro-Pro-Gln-Gly-Gly-Arg-Pro-Ser-Arg-Pro- Pro-Gln by conventional methods. The amino terminal ten residues of P-H were the same as those of proline-rich peptides P-D, P-E, and P-F reported previously. Comparison of the amino acid sequences between P-H and P-D revealed that there are two deletion parts and several amino acid substitutions in the sequence of P-H. Homology between P-H and P-D was as high as 70%.

Amino Acid Sequence↗
PubMed1983

Conformational study of the salivary proline-rich polypeptides.

The conformational study of three proline-rich polypeptides of human whole saliva, with known primary structures, was performed by CD and 1H-n.m.r. spectra measurements. All these polypeptides contained more than four consecutive prolyl residues in their amino acid sequences. The occurrence of the poly-L-proline form II conformation in their structures was demonstrated with two of these polypeptides. The continuous prolyl residues in the third was suggested to take the same structure as the others.

Circular Dichroism↗
PubMed1983

Immunohistochemical demonstration of salivary proline rich peptide P-C like immunoreactivity in human pancreatic B-cells.

Antisera against proline rich peptide P-C, recently isolated from human whole saliva were raised in rabbits by injections of peptide P-C-BSA conjugates. Immunohistochemical study using the antisera was carried out on human salivary glands, gut and pancreas. The results showed that peptide P-C like immunoreactivity was present not only in the salivary glands but also in the pancreatic islets, though not in the gut. Furthermore, immunostaining of adjacent thin sections revealed that cells reacting with antisera against peptide P-C were identical to those reacting with insulin antisera. As the antisera against peptide P-C did not have any cross-reactivities to insulin, glucagon, somatostatin, pancreatic polypeptide, VIP and human C-peptide, the antisera were considered to recognize specifically either peptide P-C related antigen or peptide P-C itself in human pancreatic B-cells. A novel substance, peptide P-C like immunoreactivity, may be present in pancreatic B-cells independent of pro-insulin and insulin. Morphological similarity between the salivary glands and the pancreas has been reported, and amylase, kallikrein and glucagon are present in both. These findings seem to suggest some functional relation between the pancreas and salivary glands. Detection of peptide P-C like immunoreactivity in the pancreas and salivary glands would be a additional support for this idea. Although it is suggested that peptide P-C like immunoreactivity in pancreatic B-cells may play some role in the function of B-cells, its exact pathophysiological role remains obscure.

Animals↗
PubMed1982

Fractionation and characterization of basic proline-rich peptides of human parotid saliva and the amino acid sequence of proline-rich peptide P-E.

Basic proline-rich peptides of human parotid saliva were fractionated and characterized. The amino acid sequence of one of the purified peptides, P-E, was determined to be (formula: see text). The results demonstrate the repetitiveness of the partial sequence within the molecule and the occurrence of structures common to those of other salivary polypeptides such as P-C and Protein C.

Adult↗
PubMed1982

[Experimental and clinical studies of cefmenoxime in the field of obstetrics and gynecology].

The study group was organized to evaluate the usefulness of cefmenoxime (CMX) injection, a new synthetic cephalosporin, for the treatment of infections in the field of obstetrics and gynecology. Fundamental and clinical studies were made by the society and the following results were obtained. 1. The peak distribution of CMX's MIC for E. coli, Klebsiella sp., Enterobacter sp., Bacteroides sp. and Peptococcus sp. isolated from obstetrical and gynecological infections with relatively high frequencies area 0.1, less than or equal to 0.05, 0.2, 3.13, 1.56 micrograms/ml, respectively, with an inoculation of 10(6) cells/ml. 2. When 1 g of CMX is administered by intravenous drip infusion for 1 hour, the maximum concentrations in various tissues of female genital organs were as follows: 14.2 and 13.2 micrograms/g in ovary and oviduct, respectively, at 1.20 hours after the start of administration, and 16.9 and 26.3 micrograms/g in corpus uteri and cervix uteri, respectively, after 1 hour. As for the transfer to the exudate in the pelvic dead cavity, the peak concentration was 15.6 micrograms/ml after 2.13 hours. 3. In the clinical studies, CMX was given to 258 cases with female genital organ infections and others. As for the clinical effects, with exclusion of 3 cases in which other antibiotics are concomitantly used, responses were excellent in 76 cases, good in 162 cases and poor in 17 cases, among 255 cases in total. The efficacy rate was 93.3%. The efficacy rates by diseases were 97.1% (68/70) for intrauterine infections, 88.8% (79/89) for intrapelvic infections, 98.4% (62/63) for adnexitis, and 100% (23/23) for infections of external genital organs. As for the clinical effects on causative bacteria, the efficacy rates were 100% (19/19) for single infections due to Gram-positive bacteria, 94.8% (55/58) for single infections due to Gram-negative bacteria, and 88.2% (15/17) for single infections due to anaerobic bacteria. And its efficacy rates were 89.6% (69/77) for mixed infection cases. Side effects were observed in 2 cases (0.8%); 1 case with eruption, and 1 case with diarrhea and vomiting. As for abnormal laboratory findings, lower white blood cell count was observed in 2 cases and elevation of the values regarding hepatic functions in 9 cases. All cases were returned to the normal after the completion of the administration. Cefmenoxime showed a satisfactory clinical efficacy and a potent bacteriological effect in treatment of the infections in the field of obstetrics and gynecology, and it has been concluded that cefmenoxime will be useful addition to the antibiotics for the therapy of these infections.

Adolescent↗