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Biomedical subjects

Y Kuboki

Publications and source records attributed to Y Kuboki.

At least 127 records · Page 7Linked to original sources
PubMed1982

Collagen structural microheterogeneity and a possible role for glycosylated hydroxylysine in type I collagen.

A three-chained peptide from type I collagen, crosslinked by hydroxyaldolhistidine, has been isolated from a tryptic digest of 5 M guanidine.HCl-insoluble bovine skin collagen (a small but as yet unknown percentage of the total collagen in whole skin). OsO(4)/NaIO(4) specifically cleaved the crosslink at its double bond into a two-chained crosslink peptide and a single peptide. The sequence of the two-chained peptide containing the bifunctional crosslink was determined after amino acid analysis of the separated peptides. The crosslink consists of an aldehyde derived from hydroxylysine-87 in the aldehyde-containing cyanogen bromide fragment alpha1CB5(ald) and an aldehyde derived from the lysine in the COOH-terminal nonhelical region of the alpha1CB6(ald) fragment. The alpha1CB6(ald) portion of the peptide exhibited structural microheterogeneity, containing the inverted sequence Ala-Lys-His instead of the normal sequence Lys-Ala-His. This indicates that another structural gene exists for alpha1(I) chain. The original three-chained peptide did not contain any glycosylated hydroxylysine or glycosylated hydroxyaldolhistidine. The lack of glycosylation of hydroxylysine-87 in alpha1CB5, which is usually glycosylated, allowed formation of the aldehyde, and this, coupled with the sequence inversion, may have allowed formation of the nonreducible crosslink hydroxyaldolhistidine. We suggest that the role of glycosylation, a posttranslational modification, of specific hydroxylysine residues is to prevent their oxidative deamination to aldehydes, thereby precluding formation of complex stable crosslinks. Complex crosslinks would decrease the rate of collagen turnover. The decrease, with time, would increase the population of stable crosslinked collagen molecules, which would eventually accumulate with age.

Amino Acid Sequence↗
PubMed1981

Comparative collagen biochemistry of bovine periodontium, gingiva, and dental pulp.

Cross-linking patterns of the collagen from bovine gingiva, periodontium, and dental pulp were analyzed chromatographically. The ratios of two main cross-links, dihydroxylysinonorleucine to hydroxylysinonorlecuine, were 0.18, 0.31, and 0.49 for the bovine gingiva, periodontium, and dental pulp collagen, respectively. These ratios are similar to that of skin collagen rather than that of bone and dentin collagen.

Amino Acids↗
PubMed1981

Studies on prolidase deficiency with a possible defect in collagen metabolism.

Skin collagen of a female patient with prolidase deficiency was examined for the distribution of borohydride-reducible cross-links and the proportion of type III to type I collagen. Patient's skin contained after reduction more dihydroxylysinonorleucine relative to hydroxylysinonorleucine and type III collagen than expected for normally matured skin. These findings suggest that collagen of the patient's skin failed to follow a time-related normal maturation process and the collagen metabolism was disturbed. The composition of urinary collagen metabolites was also unusual. On the the other hand, her asymptomatic brother with prolidase deficiency showed the normal urinary compositon of collagen matabolites. It is suggested that prolidase deficiency and defect in collagen metabolism independent of it are both responsible for clinical manifestation.

Collagen↗
PubMed1981

Location of an intermolecular crosslink in bovine bone collagen.

A peptide containing 59 amino acid residues with a stoichiometric amount of dihydroxylysinonorleucine (0.7 mole) and hydroxylysinonorleucine (0.2 mole) was isolated from reduced 3H labelled bovine bone collagen sequentially cleaved with CNBr and trypsin. Further cleavage of the isolated crosslinked peptide with periodate yielded a radioactive peptide of 45 residues and a non-radioactive peptide of 16 residues. From the characteristic amino acid composition of these peptides it was deduced that the peptide was derived from an intermolecularly crosslinked region between lysyl or hydroxylysl residues in the carboxy-terminal extension of alpha 1-CB6 (17C residue) and alpha 1-CB5 (87th residue). This finding supports the observation that the alpha 1-CB6 peak was prominent on carboxymethyl cellulose chromatography of the CNBr digest of bone collagen only after limited pepsin digestion, and is consistent with the results obtained from a smaller crosslinked peptide previously isolated from calf bone collagen.

Amino Acids↗
PubMed1980

Dentinogenesis imperfecta: evidence of qualitative alteration in the organic dentin matrix.

Deciduous teeth affected by dentinogenesis imperfecta were obtained from two patients with osteogenesis imperfecta. Electronmicroscopy of the dentin revealed some structural alterations. The striation of the collagen fibrils was not clear, and the crystals were less dense than in normal dentin. The amino acid analysis of dentin collagen was slightly different from normal dentin. There were slight increases in the amounts of hydroxylysine, serine and acidic acids. On the other hand, lysine and arginine were reduced. The elevation of hexosyllysine content and an increase of carbohydrate were also observed. These results indicate that either dentin collagen is altered, or noncollagenous matrices associated with collagen are increased in dentinogenesis imperfecta dentin.

Adolescent↗
PubMed1979

Detection of collagen degradation products from subcutaneously implanted organic bone matrix.

Demineralized bovine bone powder was reduced with NaB3H4 to label the collagen crosslinks with tritium. The powder was enclosed in small nylon mesh pouches and implanted subcutaneously into rats for 3 weeks. Histological examinations revealed that multinuclear giant cells accumulated around the bone matrix, some in Howship's lacunae. Collagenous peptides containing intermolecular crosslinks were detected in the urea-soluble fraction extracted from the implant. Two crosslink-containing peptides were isolated from a dialyzable fraction: one contained dihydroxylysinonorleucine and the other hydroxylysinonorleucine. Both peptides had molecular weights of approximately 1000 estimated from the elution positions of gel filtration chromatography; and both had similar quantitative compositions of amino acids. There were no homologous peptides detected in a control experiment of the reduced bone matrix which was incubated in vitro with buffered saline for 1 week at 37 degrees C.

Animals↗
PubMed1979

Proteochondroitin sulfate synthesized in cartilages induced in vivo and in vitro by bone matrix gelatin.

Implanted allogeneic demineralized bone matrix gelatin induced sequential development of cartilage and bone in the recipient rat muscle tissue. Proteoglycans of the implants labeled in vivo with [35S]sulfate at different stages of development were analyzed by sucrose density gradient centrifugation. The major proteoglycan synthesized in day-5 implant, just prior to onset of chondrogenesis, was a dermatan sulfate-containing proteoglycan with relatively slow sedimentation rate. Additionally, a small amount of a faster sedimenting component could be detected. The faster sedimenting proteoglycan, in which chondroitin 4-sulfate accounted for 85% of total radioactivity, became predominant in day-10 sample when cartilage formation was maximal. By day 30, when cartilage had been replaced by newly formed bone, the synthesis of this faster sedimenting component had ceased. A similar, if not identical, proteoglycan was found to be a major one synthesized by the in vitro-induced cartilage. This proteoglycan was smaller in overall size and shorter in length of its chondroitin sulfate chains than a major proteoglycan component obtained from neonatal rat epiphyseal cartilage. Concurrent with these changes in proteoglycan type, there appeared to be a change in collagen type, since type II collagen, in addition to type I collagen, was synthesized in day-10 implant. These results indicate that the proteoglycan can be used as a molecular marker for chondrogenesis by bone matrix gelatin.

Abdominal Muscles↗
PubMed1979

Calcium-specific precipitation of dentin phosphoprotein: a new method of purification and the significance for the mechanism of calcification.

Calcium, but not magnesium or strontium ions, specifically induce the precipitation of dentin phosphoprotein, which is reversibly solubilized by EDTA. This finding is very useful in pruifying dentin phosphoprotein of either a free or matrix-bound type. Bovine dentin phosphoproteins, thus isolated, contain a minimal amount of contaminant protein, unlike previous preparations.

Amino Acids↗
PubMed1978

Hydroxyapatite-reactive salivary protein revealed by iso-electrofocusing electrophoresis.

Salivary protein involvement in the formation of acquired enamel pellicle, so far, has been discussed in terms of hydroxyapatite (HA)-reactive salivary proteins only from the parotid gland. This study was undertaken to seek this type of protein in the human whole (mixed) saliva and to investigate its normal and pathological variations. Several kinds of hydroxyapatite, either biogenous or synthesized by solid phase reaction, were used as a powder (250 mesh). HA was incubated with concentrated whole saliva at 25 degrees for 30 min. After centrifugation and filtration salivary proteins were analysed on a Multiphor isoelectrofocusing gel electrophoresis. The control salivary proteins were separated into three major groups; acidic (A1-A8), neutral neutral (N1-N4), and basic (B1-B3) isoelectric point (pI). In the HA incubated sample, one of the major neutral bands (NI) preferentially disappeared at about pI 7.5. This NI band was missing or scarce in the parotid saliva and had an amino acid composition rich in glycine, lysine, serine, glutamic acid, aspartic acid, and histidine. This protein was considered to be one of the major HA-reactive proteins in human whole saliva.

Adsorption↗
PubMed1977

Collagen biochemistry of the two layers of carious dentin.

The amino acid composition and intermolecular cross links of collagen fibers in the two layers of carious dentin, differentiated by a 0.5% basic fuchsin-propylene glycol-stain, were biochemically investigated. No difference in the pattern of amino acid composition of collagen fibers was found between the first and second layers of carious dentin and the sound dentin. However, obvious differences in the intermolecular cross links of collagen fibers were found between the three layers. Namely, compared with the sound dentin, the second layer of carious dentin had decreased cross links and increased precursors. This change is considered to be reversible. Contrastingly, in the first layer, both the cross links and the precursors remarkably decreased. In addition, the hexitollysines (protein-saccharide compounds probably related to bacterial metabolism) were found and several peaks of unknown materials appeared. This indicates irreversible destruction of cross-linkage in the first layer of carious dentin.

Amino Acids↗
PubMed1976

Aging of human bone and articular cartilage collagen: changes in the reducible cross-links and their precursors.

The age-dependent changes in reducible collagen cross-links, Schiff bases and their precursors were followed for human bone and articular cartilage throughout the whole life span from 3 to 89 years of age. With aging, the reduced Schiff bases dihydroxylysinonorleucine remarkable decreased, wheras hexitollysine peaks increased significantly in both collagens. Dihydroxynorleucine, the precursor of the cross-link, was found to increase slightly with age. But the changes in hydroxylysinonorleucine and lysinonorleucine were comparatively small. These changes were discussed in relation to the increased insolubility observed in both collagens at higher age.

Adolescent↗