Biomedical subjects

Shingo Tajima

Publications and source records attributed to Shingo Tajima.

24 records · Page 2Linked to original sources

PubMed2002

Type XVI collagen is expressed in factor XIIIa+ monocyte-derived dermal dendrocytes and constitutes a potential substrate for factor XIIIa.

We have previously reported that connective tissue cells in the superficial dermis preferentially express alpha1(XVI) collagen rather than those in the lower dermis. Double immunofluorescence labeling using the antibodies for alpha1(XVI) collagen and factor XIIIa (plasma transglutaminase), which is a marker of dermal dendrocytes, demonstrated that both antibodies reacted with the same cells in the superficial dermis of normal skin as well as the lesional skins of dermal dendrocyte-related disorders, dermatofibroma, and psoriasis. Dermal dendrocytes are considered to be established by a culture of peripheral blood monocytes in the presence of granulocyte macrophage-colony stimulating factor and interleukin-4. Reverse transcription--polymerase chain reaction, metabolic labeling, and immunofluorescence studies demonstrated that treatment of CD14+ peripheral blood monocytes with granulocyte macrophage-colony stimulating factor/interleukin-4 over a period of 8 d resulted in the induction of alpha1(XVI) collagen as well as factor XIIIa. The physiologic significance of colocalization of alpha1(XVI) collagen and factor XIIIa in the tissue and their coordinate induction in CD14+ monocyte-derived dendritic cells in vitro was studied. Considerable incorporation of [3H]putrescine by factor XIIIa into recombinant noncollagenous domain (NC) 11 but not into collagenous domain (COL) 1.NC1 domain of the alpha1(XVI) polypeptide was found. Incubation of recombinant NC11 of alpha1(XVI) polypeptide with factor XIIIa in vitro produced a covalent cross-linking complex on sodium dodecylsulfate-polyacrylamide gel electrophoresis. The results indicate that alpha1(XVI) collagen is constitutively expressed by most dermal dendrocytes in the skin and dendritic cells differentiated from peripheral blood monocytes in vitro. Type XVI collagen is expressed in factor XIIIa+ dermal dendrocytes and may form an intermolecular cross-linking through NC11 domain by the reaction catalyzed by factor XIIIa contributing to the structural integrity of factor XIIIa+ dendritic cell-rich tissues.

Adult↗

PubMed2002

Advanced glycation end product-modified beta2-microglobulin is a component of amyloid fibrils of primary localized cutaneous nodular amyloidosis.

Primary localized cutaneous nodular amyloidosis is a rare form of cutaneous amyloidosis. Amyloid fibrils in primary localized cutaneous nodular amyloidosis have been reported to be originated from immunoglobulin light chains. Immunohistochemical studies on the lesional skins of four patients with primary localized cutaneous nodular amyloidosis demonstrated that amyloid deposits of all cases showed a positive reaction with the antibodies for beta2-microglobulin and advanced glycation end products as well as immunoglobulin light chain (kappa or lambda). No beta2-microglobulin and advanced glycation end product immunoreactivity was found in the amyloid deposits of other primary localized cutaneous amyloidosis (lichen amyloidosis and macular amyloidosis). Double immunofluorescence study of the lesional skin of primary localized cutaneous nodular amyloidosis showed that anti-kappa light chain, anti-beta2-microglobulin and anti-advanced glycation end product antibodies mostly reacted with the same area of amyloid deposit. Amyloid proteins were sequentially extracted with distilled water from one case of primary localized cutaneous nodular amyloidosis and recovered in the five water-soluble fractions (fractions I-V). Immunoblot assay of amyloid fibril proteins demonstrated that immunoreactive polypeptides with anti-kappa light chain antibody (29 kDa) and with anti-beta2-microglobulin antibody (12 kDa) were detected in fractions I-V, whereas immunoreactive polypeptide with anti-advanced glycation end product antibody (12 kDa) was detected exclusively in fractions III-V but not in fractions I and II. Two-dimensional polyacrylamide gel electrophoresis revealed that 12 kDa polypeptide in fractions I and II was electrophoretically identical with authentic beta2-microglobulin and that beta2-microglobulin in fractions III-V was advanced glycation end product-modified beta2-microglobulin with more acidic pI value. These results indicate that beta2-microglobulin is another major component of amyloid fibrils in primary localized cutaneous nodular amyloidosis and that beta2-microglobulin in primary localized cutaneous nodular amyloidosis is partly subjected to the modification of advanced glycation end product.

Aged↗

PubMed2002

Coexistence of pseudoxanthoma elasticum-like papillary dermal elastolysis and linear focal dermal elastosis.

An 89-year-old Japanese woman had pseudoxanthoma elasticum-like papillary dermal elastolysis on the neck and linear focal elastosis on the flexor aspects of the legs and thighs. The lesions of both diseases had similar histologic patterns-loss of elastic fibers in the papillary dermis and accumulation of normal-appearing elastic fibers in the subpapillary or mid dermis. Immunohistochemical analysis showed elastin, and microfibril-associated proteins (fibrillin 1 and 2 and microfibril associated glycoprotein 1 and 4) were absent or decreased in the papillary dermis and present in the accumulated elastic fibers in both lesions. The association of 2 diseases on different areas of the same patient and histologic and immunohistologic similarities between the diseases suggest that, despite the clinical differences, both diseases are closely related.

Aged↗

PubMed2002

A variant of acrokeratoelastoidosis in systemic scleroderma: report of 7 cases.

We describe acrokeratoelastoidosis-like lesions on the palms of the patients with systemic scleroderma. Histology showed a focal hyperkeratosis with or without epidermal concavity, regular acanthosis, and hyalinization of collagen fibers and, in some cases, fragmentation and diminution of elastic fibers in the deep dermis. A slight degree of fibrotic change of collagen in the uninvolved neighboring skin was found in one case. The lesions were found in 7 of 26 patients with systemic scleroderma who were analyzed here, and were not found in the unrelated connective tissue disorders (n = 32) and normal controls (n = 27). The cause of the unique skin lesions may be related to the altered connective tissue metabolism similar to that of systemic scleroderma.

Adult↗

PubMed2002

Polycystic kidney disease associated with cervical arteriovenous shunt and bilateral jugular vein occlusion.

A 59-year-old man with abnormal vascular features (intracranial aneurysm, a cervical arteriovenous shunt, bilateral internal jugular vein occlusions, and left transverse sinus hypoplasia), as well as left optic atrophy was suspected to have familial polycystic kidney disease. The possibility of autosomal dominant polycystic kidney disease complicated by Ehlers-Danlos syndrome type IV due to the coexistence of vasculopathy and polycystic kidneys was considered. However, the negative results of a skin fibroblast culture rendered the diagnosis of Ehlers-Danlos syndrome type IV unlikely. The cause of left optic atrophy in our patient remains unclear although it was suspected to be a secondary consequence of papilledema, which was caused by intracranial hypertension.

Arteriovenous Fistula↗

PubMedDate not supplied

Amyloid deposition of systemic myeloma-associated amyloidosis excludes actinic elastotic material.

We report a 65-year-old Japanese man presenting with myeloma-associated systemic amyloidosis. A biopsy specimen taken from the purpuric papules on the periorbital area showed the presence of both amyloid and elastotic materials (actinic elastosis) in the upper dermis. Amyloid deposition and altered elastotic fibers were clearly bordered and never colocalized, and amyloid materials appeared to exclude elastotic materials. The mechanism of this phenomenon is discussed.

Aged↗