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Gene. 2000 Oct 3;256(1-2):229-36.
Affinity selection of cDNA libraries by lambda phage surface display.

Niwa M, Maruyama H, Fujimoto T, Dohi K, Maruyama IN.

Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037, USA.

Bacteriophage lambda surface display was used to isolate cDNA clones encoding autoantigens recognized by sera from patients with Sjogren's syndrome (SS). We made cDNA libraries from human HeLa and HepG2 cells, using the expression vector lambdafoo. By repeating affinity selection of the libraries with the sera immobilized in microtiter wells, we isolated three clones that encode previously unknown antigens as well as four clones previously known as SS autoantigens. The newly identified autoantigens include TRK-fused gene product (TFG), survival motor neuron gene product (SMN) and pM5, which has a similarity to the metal-binding domain of human fibroblast collagenase. Thus, the bacteriophage lambda surface display is powerful for isolating cDNA clones by affinity screening.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11054552&dopt=Abstract

J Endocrinol. 2000 Nov;167(2):305-13.
Estrogen modulates osteoblast proliferation and function regulated by parathyroid hormone in osteoblastic SaOS-2 cells: role of insulin-like growth factor (IGF)-I and IGF-binding protein-5.

Nasu M, Sugimoto T, Kaji H, Chihara K.

Third Division, Department of Medicine, Kobe University School of Medicine, 7-5-1 Kusunoki-cho, Chuo-ku, Kobe 650, Japan.

Although there is clinical evidence showing that combined therapy with parathyroid hormone (PTH) and estrogen is additively effective in increasing the bone mass of patients with osteoporosis, the mechanism of the interaction between these hormones remains unclear. The present study was performed to determine whether estrogen would affect osteoblast proliferation and function modulated by PTH in human osteoblastic SaOS-2 cells. Human PTH-(1-34) significantly inhibited [(3)H]thymidine (TdR) incorporation, which was attenuated by 24 h pretreatment with 10(-10) to 10(-7) M 17 beta-estradiol (17 beta-E(2)) in a concentration-dependent manner. PTH significantly stimulated alkaline phosphatase (ALP) activity, collagen synthesis and type-1 procollagen mRNA expression after pretreatment with 17 beta-E(2 )in these cells. Tamoxifen, an anti-estrogen, antagonized these 17 beta-E(2)-induced effects. Pretreatment with insulin-like growth factor-I (IGF-I) mimicked estrogen action, and coincubation of 3 microg/ml anti-IGF-I antibody antagonized the effects of 17 beta-E(2 )as well as those of IGF-I. In the presence of 17 beta-E(2 )pretreatment, PTH strongly stimulated IGF-binding protein (IGFBP)-5 mRNA expression in these cells, and recombinant IGFBP-5 increased type-1 procollagen mRNA expression and ALP activity. In conclusion, estrogen attenuates PTH-induced inhibition of osteoblast proliferation and PTH stimulates osteoblast function in the presence of estrogen pretreatment. IGF-I and/or IGFBP-5 seemed to be involved in the estrogen-induced modulation of PTH action on osteoblast proliferation and function.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11054645&dopt=Abstract

Int J Cancer. 2000 Nov 1;88(3):417-23.
Expression of collagenase-3 (matrix metalloproteinase-13) in transitional-cell carcinoma of the urinary bladder.

Bostrom PJ, Ravanti L, Reunanen N, Aaltonen V, Soderstrom KO, Kahari VM, Laato M.

Department of Surgery, Turku University Central Hospital, Finland.

Expression of collagenase-3 [matrix metalloproteinase-13 (MMP-13)] has been previously demonstrated in squamous-cell carcinomas of both the head and neck and the vulva, cutaneous basal-cell carcinomas, chondrosarcomas and melanomas. Using in situ hybridization, MMP-13 mRNA expression was detected in 13 of 23 (52%) urinary bladder transitional-cell carcinomas (TCCs). Expression was restricted to cells in the invading edges of tumors. No expression of MMP-13 mRNA could be detected in normal urothelium. As detected by immunohistochemistry, MMP-13 protein showed an expression pattern similar to that of MMP-13 mRNA. Expression of MMP-13 mRNA and protein was also detected in 2 bladder carcinoma cell lines (RT4 and T24). In these cell lines, TNF-alpha potently induced MMP-13 mRNA expression. Retinoids and a selective p38 inhibitor, SB203580, potently inhibited MMP-13 mRNA expression. Our results demonstrate MMP-13 expression in human urinary bladder carcinoma cells in vivo and in vitro and suggest that MMP-13 may serve as a marker for transformation and invasion in urinary bladder TCCs.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11054671&dopt=Abstract

J Pathol. 2000 Nov;192(3):385-95.
A light and electron microscopic study of osteogenesis imperfecta bone samples, with reference to collagen chemistry and clinical phenotype.

Sarathchandra P, Pope FM, Kayser MV, Ali SY.

Department of Experimental Pathology, Institute of Orthopaedics (University of London), Royal National Orthopaedic Hospital, Stanmore, Middlesex, HA7 4LP, UK. p.sarathchandrc.ac.uk

A detailed morphological study was carried out using light and electron microscopy on 36 bone specimens from patients suffering from osteogenesis imperfecta (OI) and 20 age- and site-matched control bone specimens. The findings were grouped into the clinical types of OI according to the Sillence classification. The morphological and ultrastructural alterations observed in OI bone correlate well with clinical severity. Thus, OI type I, the mildest type, showed the least abnormalities in bone ultrastructure. OI type IV closely resembled type I, with only minor abnormalities in the bone cells and osteoid. OI type III showed abnormalities in the structure and distribution of osteoid collagen fibrils, whilst OI type II, the lethal form, revealed many varied abnormalities such as thin cortical bone, sparse trabecular bone, increased numbers of osteoclasts and osteocytes, thin osteoid with thin collagen fibrils, and patchy mineralization. 2000 John Wiley & Sons, Ltd.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11054723&dopt=Abstract

J Neurosci Res. 2000 Nov 1;62(3):451-62.
Laminin inhibition of beta-amyloid protein (Abeta) fibrillogenesis and identification of an Abeta binding site localized to the globular domain repeats on the laminin a chain.

Castillo GM, Lukito W, Peskind E, Raskind M, Kirschner DA, Yee AG, Snow AD.

ProteoTech Inc., Kirkland, Washington 98034, USA. castillroteotech.com

beta-Amyloid protein (Abeta) is a major component of neuritic plaques and cerebrovascular amyloid deposits in the brains of patients with Alzheimer's disease (AD). Inhibitors of Abeta fibrillogenesis are currently sought as potential future therapeutics for AD and related disorders. In the present study, the basement membrane protein laminin was found to bind Abeta 1-40 with a single dissociation constant, K(d) = 2.7 x 10(-9) M, and serve as a potent inhibitor of Abeta fibril formation. 25 microM of Abeta 1-40 was incubated at 37 degrees C for 1 week in the presence of 100 nM of laminin or other basement membrane components, including perlecan, type IV collagen, and fibronectin to determine their effects on Abeta fibril formation as evaluated by thioflavin T fluorometry. Of all the basement membrane components tested, laminin demonstrated the greatest inhibitory effect on Abeta-amyloid fibril formation, causing a ninefold inhibition at 1 and 3 days and a 21-fold inhibition at 1 week. The inhibitory effects of laminin on Abeta fibrillogenesis occurred in a dose-dependent manner and were still effective at lower concentrations. The inhibitory effects of laminin on Abeta 1-40 fibril formation was confirmed by negative stain electron microscopy, whereby laminin caused an almost complete inhibition of Abeta fibril formation and assembly by 3 days, resulting in the appearance of primarily amorphous nonfibrillar material. Laminin also caused partial disassembly of preformed Abeta-amyloid fibrils following 4 days of coincubation. Laminin was not effective as an inhibitor of islet amyloid polypeptide fibril formation, suggesting that laminin's amyloid inhibitory effects were Abeta-specific. To identify a potential Abeta-binding site(s) on laminin, laminin was first digested with V8, trypsin, or elastase. An Abeta-binding elastase digestion product of approximately 120-130 kDa was found. In addition, a approximately 55 kDa fragment derived from V8 and elastase-digested laminin interacted with biotinylated Abeta 1-40. Amino acid sequencing of the approximately 55 kDa fragment identified a conformationally dependent Abeta-binding site within laminin localized to the globular repeats on the laminin A chain. These studies demonstrate that laminin not only binds Abeta with relatively high affinity but is a potent inhibitor of Abeta-amyloid fibril formation. In addition, further identification of an Abeta-binding domain within the globular repeats on the laminin A chain may lead to the design of new therapeutics for the inhibition of Abeta fibrillogenesis. 2000 Wiley-Liss, Inc.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11054814&dopt=Abstract

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