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The endometrial tissue, obtained from the infertile patient, was cultured on the basement membrane extract with serially obtained maternal serum

Munro Mullen
· 3 min read
The endometrial tissue, obtained from the infertile patient, was cultured on the basement membrane extract with serially obtained maternal serum

Addition of the maternal serum after proper administration of pFSH, high estrogen conditions were made in the culture dishes. These conditions increased the height of the glandular structure and relatively decreased the area of the surface epithelium. Decreased the area of surface epithelium affected the rate of the attachment. Endometrial cell culture system associated with functional and morphological characteristics was established. Serial observation of the endometrial cells in this system revealed the rabbit and the human implantation process, and the embryo-endometrial interaction.(ABSTRACT TRUNCATED AT 400 WORDS)A novel variant of acquired epidermolysis bullosa with autoantibodies against the central triple-helical domain of type VII collagen.

Shimizu H, Tanaka T, Kishiyama K, Höpfner B, Takahashi H, Iizuka H, Epidermolysis bullosa acquisita and bullous systemic lupus erythematosus are autoimmune bullous disorders, with tissue-bound and circulating autoantibodies reactive with the noncollagenous NC1 domain of type VII collagen (C-VII). Here, we describe a novel acquired bullous dermatosis with autoantibodies against the triple-helical domain of C-VII. Three patients, all Japanese children, presented with widespread inflammatory tense blisters. Histologically, subepidermal tissue separation was noted with inflammatory infiltrate in the superficial dermis. Direct immunofluorescence staining revealed linear IgG/C3 deposits along the dermal-epidermal junction. Circulating IgG anti-basement membrane zone autoantibodies stained the dermal side of normal skin separated with 1 M NaCl. Direct and indirect immunoelectron microscopy using colloidal gold labeling showed that patient sera reacted with anchoring fibrils.

The gold particles were localized both near the lamina densa and on the central banded portion of the fibrils. The sera reacted with C-VII in immunoblots. Epitope analyses with natural and recombinant fragments of C-VII disclosed that the sera did not recognize the NC1 domain of C-VII, but the central triple-helical domain of this anchoring fibril protein. Thus,  the ordinary cleanser  show a hitherto unrecognized variant of epidermolysis bullosa acquisita, with autoantibodies against epitopes in the collagenous domain of C-VII.Immunoidentification of type XII collagen in embryonic tissues.We have generated a monoclonal antibody against a synthetic peptide whose sequence was derived from the nucleotide sequence of a cDNA encoding alpha 1(XII) collagen. The antibody, 75d7, has been used to identify the alpha 1(XII) chain on immunoblots of SDS-PAGE tendon extracts as a 220-kD polypeptide, under reducing conditions.

squalane oil -terminal amino acid sequence analysis of an immunopurified cyanogen bromide fragment of type XII collagen from embryonic chick tendons gave a single sequence identical to that predicted from the cDNA, thus confirming that the antibody recognizes the type XII protein. Immunofluorescence studies with the antibody demonstrate that type XII collagen is localized in type I-containing dense connective tissue structures such as tendons, ligaments, perichondrium, and periosteum. With these data, taken together with previous results showing that a portion of the sequence domains of type XII collagen is similar to domains of type IX, a nonfibrillar collagen associated with cross-striated fibrils in cartilage, we suggest that types IX and XII collagens are members of a distinct class of extracellular matrix proteins found in association with quarter-staggered collagen fibrils.Role of fibrillar structure of collagenous carrier in bone sialoprotein-mediated matrix mineralization and osteoblast differentiation.Medical School and Children's Hospital, Boston, MA 02115, USA.To investigate the effects of the microstructure of collagenous carriers on the in vivo function of bone sialoprotein (BSP) in mineralization and osteoblast differentiation, we examined the ultrastructure of reconstituted type I collagen (collagen) and heat-denatured collagen (gelatin) and the in vivo responses to purified bone-derived BSP that was implanted with collagen or gelatin into surgically created 8-mm rat calvarial bone defects. Scanning and transmission electron microscopies revealed that the collagen displayed a fine fibrillar structure with interconnecting spaces between the fibrils/fibers, while the gelatin completely lost this unique three-dimensional structure after denaturation.

The rates of in vivo release of BSP from the collagen scaffold were significantly lower than those from the gelatin. Collagen-BSP, but not gelatin-BSP, induced early mineral deposition in the matrix of proliferating repair cells in the calvarial defects at approximately 4-7 days after implantation. Expression levels of osteoblast markers, alkaline phosphatase activity and amounts of new bone synthesized in the collagen-BSP treated defects were significantly greater than that in the gelatin-BSP treated defects (p<001).