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Biomedical subjects

L Napolitano

Publications and source records attributed to L Napolitano.

At least 37 records · Page 2Linked to original sources

[Skeletization of the inferior mesenteric artery in colorectal surgery. Current considerations].

Anastomotic dehiscence after colon resection is the most frequent complication in colon surgery and the main cause of post-operative death. In the light of anatomical peculiarities of the blood supply to the rectum, it would appear that in atherosclerotic patients with impairment of hypogastric arteries (80% in authors' series out of 200 atherosclerotic subjects) inferior mesenteric artery ligature, determining vascularization of the rectal ampulla by the distal vessels alone, results in an insufficient supply in case of colo-rectal anastomosis. A series of 15 cases of cancer of the left and sigmoid colon, treated with left hemicolectomy, preservation and peeling of the inferior mesenteric artery, is reported. In the follow-up ranging from 6 months to 5 years, no anastomotic dehiscence was observed and only one case (7.5%) presented hepatic recurrence after two years. The other patients are all alive and disease free.

Aged↗

[Medullary carcinoma of the thyroid].

Medullary thyroid carcinoma represents 4-8% of thyroid malignancies; regional nodal involvement is commonly found, even at the time of first surgical approach. In these patients after surgical resection, other therapeutic choices are really limited. The Authors evaluated their experience in the period 1981-1994, concerning 14 patients, 9 females and 5 males, all affected with sporadic MTC. Diagnosis was preoperative in 10 patients and intraoperative in 4; as for the staging: in 8 patients the tumor resulted confined to the thyroid, while in the remaining 6 patients it was extra-thyroidal. In 5 patients a total thyroidectomy with regional lymphadenectomy was performed, with in 6 patients a total thyroidectomy with cervico-mediastinic total lymphadenectomy was achieved. Survival was evaluated with a short, follow-up (3 months) and calculated using the K-Mayer method. Average survival was: 5 years in patients undergoing only total thyroidectomy; 3 years and 1 month in patients undergoing total thyroidectomy and lymphadenectomy; 6 months in patients undergoing no treatment at all. Among the factors negatively affecting patients survival, the Authors pointed out: metastasis occurrence; incomplete resection and mediastinal metastasis. In conclusion surgical resection (total thyroidectomy) associated with radical lymphadenectomy resulted to be a good approach. However, prognostic factors require further investigation.

Adult↗

Human alpha S1-casein like protein: purification and N-terminal sequence determination.

Casein components of human milk are generally reported to belong to the beta- and kappa-groups. In this research human casein fraction was obtained from pooled mature milk, either by ultracentrifugation or by acid precipitation. In both cases a minor component with a slightly higher mobility in SDS-PAGE than beta-casein was identified. The protein was purified to homogeneity, the N-terminal sequence of the first 14 amino acid residues of this new human casein subunit shows a high degree of homology with the alpha s1-casein sequences from other species.

Amino Acid Sequence↗

The amino-acid sequence of two isoforms of alpha-lactalbumin from donkey (Equus asinus) milk is identical.

The complete primary structure of donkey alpha-lactalbumin A and B has been determined by sequencing of the peptides obtained after tryptic, Glu-C proteinase or cyanogen bromide cleavage. Although preparative purification of alpha-lactalbumin by flat-bed isoelectric focusing gave two protein fractions A and B, their amino-acid sequence revealed no differences. Donkey alpha-lactalbumin shows two, four and five differences in comparison to the horse alpha-lactalbumin A, B and C. Thus donkey alpha-lactalbumin is homogeneous and belongs to the horse A-type variant.

Amino Acid Sequence↗

[Complications during preoperative embolization in intracranial meningioma].

We report a rare case of meningioma of the parieto-occipital convexity accompanied by hemorrhage in the tumor and in the subdural space that occurred while pre-operative embolization was being applied. The patient, a 48 year old woman, presented sudden headache and, in a few minutes, comatose status and decerebrate rigidity. A quick diagnosis with CT-scan of acute intratumoral and subdural hemorrhage and a rapid intervention on the patient led to complete recovery. The possible reason for the hemorrhage is the sudden change in blood pressure of pathologic small vessels triggered by embolization.

Brain Neoplasms↗

[Neonatal infections and premature rupture of fetal membranes].

The premature rupture of the membranes is still a cause of concern due to the related risk of infection and respiratory disorders. The study included sixty-two neonates whose mothers had ruptured their membranes for at least 48 hours (group A) and 42 neonates with a high risk of infection (low birth weight, prematurity) (group B) in order to assess whether antibiotic prophylaxis used in pregnant women with premature rupture of the membranes is sufficient to reduce the risk of severe neonatal infection. The results obtained show that there is an increased frequency of RDS, jaundice and mortality in group A, whereas in group B there was a greater frequency of sepsis and urinary tract infections. Antibiotic prophylaxis therefore allows the frequency of neonatal infections following the rupture of membranes to be reduced, thus enabling the birth to be delayed in order to induce pulmonary maturity.

Anti-Bacterial Agents↗

Plasma cortisol levels in patients with septic shock.

To investigate the endogenous adrenocortical response to sepsis, plasma cortisol concentrations were measured in 37 patients (53 +/- 3 yr of age) with septic shock. Patients were studied 11 +/- 2 h after shock commenced. Vasopressor therapy was required in 35 of 37 patients (median dopamine infusion rate of 11 micrograms/kg.min, range 3 to 74). Plasma cortisol concentrations were increased markedly (median 50.7 micrograms/dl, range 15.6 to 400) above normal values (10 to 20 micrograms/dl) in patients with septic shock. Neither patients who reversed their shock nor those who survived to hospital discharge had significantly different plasma cortisol concentrations from those who did not. Patients with Gram-positive infections had increased cortisol levels compared with those who had Gram-negative infections (median 83 micrograms/dl, range 32 to 400 vs. median 44 micrograms/dl, range 16 to 81, respectively; p less than .05). The source of infection, amount of vasopressors infused, and severity of shock were not associated with differences in cortisol concentrations. The length of time in shock before collection of the blood sample for measurements of cortisol and mean arterial pressure at the time of blood collection had significant but weak negative correlations with cortisol concentrations (p less than .05, rs = .37 and p less than .05, rs = -.40, respectively). We conclude that plasma cortisol concentrations are increased in patients with septic shock, but that the degree of increase is variable. This variability may, in part, be related to type of infection, length of time in shock, and BP at the time of blood sampling.(ABSTRACT TRUNCATED AT 250 WORDS)

Adrenal Insufficiency↗

The complete primary structure of alpha-lactalbumin isolated from pig (Sus scrofa) milk.

The complete amino-acid sequence of pig alpha-lactalbumin has been determined. It was obtained by microsequencing of the native protein and the peptides derived after tryptic or cyanogen bromide cleavage. The tryptic peptides were separated by a rapid microbore HPLC method. Pig alpha-lactalbumin is 122 amino acids long and differs from the bovine homologue by 26 exchanged residues. Of the two prolines present in bovine alpha-lactalbumin, one has been deleted in the pig structure. All previously sequenced alpha-lactalbumins have shown glutamic acid at position 49, which is known to be the active site in the homologous lysozyme c structure. This residue is replaced by phenylalanine in pig alpha-lactalbumin indicating that the pig protein is the first alpha-lactalbumin with complete loss of all lysozyme functional residues.

Amino Acid Sequence↗

Covalent structure of the minor monomeric beta-lactoglobulin II component from donkey milk.

The complete primary structure of the minor beta-lactoglobulin II component from donkey milk is presented. It has been established by amino-acid sequencing and mass-spectrometry analysis of intact protein and peptides obtained after enzymatic and chemical cleavages. The molecular mass and the pI of the protein are calculated to be 18,261 Da and 4.5 respectively. Despite the close structural similarity of the donkey and horse major beta-lactoglobulin I components, their minor beta-lactoglobulin II components show substantial differences in sequence. Most observed exchanges are clustered at residues 78-106 where only 6 amino-acid residues are conserved. The primary structure of donkey beta-lactoglobulin II reveals some unusual features of minor beta-lactoglobulins II and gives new light to the evolution of beta-lactoglobulins and other lipocalins involved in retinol binding or reproductive functions.

Amino Acid Sequence↗

Microanalysis of the amino-acid sequence of monomeric beta-lactoglobulin I from donkey (Equus asinus) milk. The primary structure and its homology with a superfamily of hydrophobic molecule transporters.

The complete primary structure of donkey beta-lactoglobulin I was determined by pulsed-liquid phase microsequencing of tryptic peptides. The protein has been isolated in monomeric form and it corresponds to monomeric beta-lactoglobulin of type I. With the inclusion of donkey beta-lactoglobulin I there are 13% common residues amongst the members of the beta-lactoglobulin family. Donkey beta-lactoglobulin I is homologous to the retinol-binding protein, bilin-binding protein and five other proteins belonging to the new superfamily of hydrophobic molecule transporters. A rapid method for peptide isolation and the strategy for microsequencing of this protein have been described.

Amino Acid Sequence↗

The primary structure of donkey (Equus asinus) lysozyme contains the Ca(II) binding site of alpha-lactalbumin.

The complete primary structure of donkey lysozyme has been established by pulsed liquid-phase sequencing of tryptic and chymotryptic peptides isolated by RP-HPLC. The positions of the Cys residues were identified by labeling the Cys residues with DABIA-reagent. Donkey lysozyme is a c-type lysozyme which is 129 amino acids long. It exhibits 50% homology to the human protein. We observe the full Ca(II) binding site suggested for the homologous alpha-lactalbumines. Although horse lysozyme has been reported to contain asparagine in position 61, which was in conflict with the three-dimensional structure of lysozyme, all other known c-type lysozymes, including donkey, contain Ser 61.

Amino Acid Sequence↗

The complete amino-acid sequence of dimeric beta-lactoglobulin from mouflon (Ovis ammon musimon) milk.

beta-Lactoglobulin from Mouflon (Ovis ammon musimon) milk has been isolated and its complete primary structure determined. This protein has been isolated in dimeric form and has a molecular mass of 37 kDa. The amino-acid sequence has been determined by microsequencing of the native protein and the peptides were obtained after tryptic cleavage. The tryptic peptides were isolated by reversed phase high-performance liquid chromatography. The primary structure of mouflon beta-lactoglobulin shows close similarity to ruminant beta-lactoglobulins. The presence of His at position 20 indicates that this protein belongs to the B-type of dimeric ovine beta-lactoglobulins. Mouflon beta-lactoglobulin is a 162 amino acid long polypeptide chain with two disulphide bridges and one free thiol group. Structural similarities to the bilin-binding protein, BG protein from olfactory epithelium and retinol-binding protein are discussed.

Amino Acid Sequence↗

beta-lactoglobulins in the mammary secretions of camel (Camelus dromedarius) and she-ass. Immunological detection and preliminary physico-chemical characterization.

The mammary secretions of a monogastric, the ass, and those of a Tylopode, the camel (camelus dromedarius), were examined by double diffusion in agarose gel against rabbit sera anti-bovine beta-lactoglobulin. Clear precipitin reactions were obtained. After immunoelectrophoresis the camel and she-ass beta-lactoglobulins showed very different electrophoretic mobilities.

Animals↗