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Biomedical subjects

T Moriguchi

Publications and source records attributed to T Moriguchi.

At least 163 records · Page 9Linked to original sources
PubMed1983

Texture of the skin graft, with special reference to the hydration state of the stratum corneum.

The water contained in the superficial portion of the stratum corneum plays an important role in keeping the skin surface soft and smooth. In an attempt to study the true nature of the "texture" of grafted skin, in vivo water sorption-desorption tests were performed on grafts, on normal skin adjacent to grafts, and on normal skin surrounding the donor sites. The results showed that skin grafted to sites other than the face maintained a functional similarity to normal skin surrounding the donor site. However, in skin grafted to the face, the functions of the stratum corneum, as measured in terms of hydration state, increased, and this was associated with an improved water-holding capacity that probably results from the effect of abundant sebum and sweat excretion in adjacent skin. From these results it is suggested that the recipient site plays an important role in determining the difference in the function of the stratum corneum, i.e., the "texture" between grafts on the face and those on other sites.

Adolescent↗
PubMed1982

Lymphadenoid structure induced by gold hypersensitivity.

An allergic sensitivity to gold earrings produced a lymphadenoid reaction with germinal centers in the dermis of the pierced earlobes of a 21-year-old woman, However, a patch test for 1% gold sodium thiomalate gave a long-lasting, clinically and histologically eczematous response. Electron microscopic and cytochemical observations showed that non-T lymphocytes and plasma cells were dominant in the dermal infiltrate of the lesions, whereas lymphocytes with convoluted nuclei (which were probably T cells) and monocytes invaded the epidermis in the patch test site. These findings suggest that continuous exposure of the dermis to gold in a sensitized person may induce a lymphadenoid cellular reaction different from the histologic findings seen after contact with the epidermis.

Adult↗
PubMed1979

Crosslink of collagen in hypertrophic scar.

It is conceivable that intramolecular and intermolecular crosslinks of collagen may be involved in the formation of hypertrophic scar, but little is known about the relationship between hypertrophic scar and crosslinks of collagen. We have isolated a new crosslinking amino acid from collagen and have named it pyridinoline. In this investigation, we examined the content of pyridinoline in human normal skin, mature scar and hypertrophic scar. An appreciable amount of pyridinoline was found in collagen of hypertrophic scar, but pyridinoline is virtually absent in collagen of normal skin.

Adolescent↗
PubMed1978

Pyridinoline, a non-reducible crosslink of collagen. Quantitative determination, distribution, and isolation of a crosslinked peptide.

Pyridinoline is a crosslink compound isolated from bovine Achilles tendon collagen. It is a 3-hydroxypyridinium derivative with three amino and three carboxyl groups (Fujimoto, D., Akiba, K., & Nakamura, N. (1977) Biochem. Biophys. Res. Commun. 76, 1124-1129). The contents of pyridinoline in collagens from various sources were determined. The pyridinoline content of bovine Achilles tendon was 0.16 residue per 1,000 residues and that of rat Achilles tendon collagen was 0.017 residue per 1,000 residues. Besides Achilles tendon collagens, pyridinoline was found in collagens from costal cartilage, rib and femoral bone of rat. It was not found in collagens from the tail tendon and skin of rat. A crosslinked, triple-chained peptide containing pyridinoline was isolated from bovine Achilles tendon collagen after digestion with pronase. Its amino acid composition suggests that the peptide may be involved in an intermolecular crosslink among a carboxyterminal sequence, a sequence near the aminoterminus and a sequence in the helical region.

Amino Acid Sequence↗
PubMed1978

Age-related changes in the content of the collagen crosslink, pyridinoline.

Pyridinoline is a crosslinking amino acid of collagen fibers. The age-related changes in the content of pyridinoline were followed for collagens from human and rat costal cartilage and Achilles tendon. The pyridinoline content of the collagens in fetal or newborn animals was very low and increased markedly with growth of the animals. In rat tissues, the pyridinoline content continued to increase after the animal had reached maturity. On the other hand, in human tissues, it began to decrease after about 30 years of age. Pyridinoline may serve as an interesting index for the aging of connective tissues.

Aging↗