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Anal Biochem. 2000 Nov 1;286(1):149-55.
Determination of matrix metalloproteinase activity using biotinylated gelatin.
Ratnikov B, Deryugina E, Leng J, Marchenko G, Dembrow D, Strongin A.
Burnham Institute, 10901 North Torrey Pines Road, La Jolla, California, 92037, USA.
Matrix metalloproteinases (MMPs) and, specifically, MMP-2 (gelatinase A) and MMP-9 (gelatinase B) are strongly associated with malignant progression and matrix remodeling. These enzymes are a subject of intensive studies involving screening of comprehensive chemical libraries of synthetic inhibitors. There is no simple method available for measurement of activity of gelatinases and related MMPs. Here, we report a simple, inexpensive, and highly sensitive assay for MMP activity. The assay performed in a 96-well microtiter plate format employs biotin-labeled gelatin (denatured collagen type I) as a substrate. Following the substrate cleavage, only the proteolytic fragments bearing biotin moieties are captured by streptavidin coated on the plastic surface and the captured fragments with at least two biotin molecules should be revealed by streptavidin conjugated with horseradish peroxidase. The frequency of lysine residues is low in collagen type I relative to the MMP cleavage sequences (PXGX). Accordingly, the majority of the cleavage products must be devoid of biotin or possess only one biotin group. Both of these types of fragments cannot be recognized by the horseradish peroxidase-streptavidin conjugate. Therefore, higher gelatinolytic activity is associated with lower signal in the assay. This 2-h assay allows identification of gelatinolytic activity of MMP-2 in concentrations as low as 0.16 ng/ml. The sensitivity of this ELISA-like assay is comparable to that of gelatin zymography, a method widely used to detect gelatinases. However, in contrast to zymography, the assay directly measures the enzymatic activity of MMP samples. The gelatinolytic activity assay permits efficient analyses and screening of the MMP inhibitor panels and allows quantitation of gelatinolytic activity of various MMPs in solution as well as on cell surfaces. 2000 Academic Press.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11038285&dopt=Abstract
J Biol Chem. 2001 Jan 12;276(2):1643-52.
Rhodocytin induces platelet aggregation by interacting with glycoprotein Ia/IIa (GPIa/IIa, Integrin alpha 2beta 1). Involvement of GPIa/IIa-associated src and protein tyrosine phosphorylation.
Suzuki-Inoue K, Ozaki Y, Kainoh M, Shin Y, Wu Y, Yatomi Y, Ohmori T, Tanaka T, Satoh K, Morita T.
Department of Clinical and Laboratory Medicine, Yamanashi Medical University, Yamanashi 409-3898, Japan.
Although glycoprotein Ia/IIa (GPIa/IIa, integrin alpha(2)beta(1)) has established its role as a collagen receptor, it remains unclear whether GPIa/IIa mediates activation signals. In this study, we show that rhodocytin, purified from the Calloselasma rhodostoma venom, induces platelet aggregation, which can be blocked by anti-GPIa monoclonal antibodies. Studies with rhodocytin-coupled beads and liposomes loaded with recombinant GPIa/IIa demonstrated that rhodocytin directly binds to GPIa/IIa independently of divalent cations. In vitro kinase assays and Western blotting of GPIa immunoprecipitates revealed that Src and Lyn constitutively associate with GPIa/IIa and that Src activity increases transiently after rhodocytin stimulation. Src specifically associates with p130 Crk-associated substrate (Cas) in a manner dependent upon Cas phosphorylation, suggesting that Src is responsible for Cas tyrosine phosphorylation. While all these phenomena occur early after rhodocytin stimulation in a cAMP-resistant manner, tyrosine phosphorylation of Syk and phospholipase Cgamma2, intracellular Ca(2+) mobilization, and platelet aggregation occur later in a cAMP-sensitive manner. Cytochalasin D, which interferes with actin polymerization and blocks receptor clustering, inhibits all the rhodocytin-mediated signals we examined in this study. We suggest that rhodocytin, by clustering GPIa/IIa, activates GPIa/IIa-associated Src, which then mediates downstream activation signals.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11038351&dopt=Abstract
Am J Med Genet. 2000 Oct 2;94(4):324-31.
Quantitative genetic analysis of circulating levels of biochemical markers of bone formation.
Livshits G, Yakovenko C, Kobyliansky E.
Research Unit-Human Population Biology, Department of Anatomy and Anthropology, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, Israel. gregcsg.tau.ac.il
Carboxyterminal propeptide of type 1 collagen (PICP) and bone Gla-protein-osteocalcin (BGP) are the most important components of the organic bone matrix and play a key role in bone formation. To investigate whether and to what extent variation of the plasma levels of these indices of bone turnover depends on genetic factors, we studied 355 adults belonging to nuclear pedigrees. Genetic analysis was carried out in 2 steps: 1) variance decomposition analysis was performed using the FISHER statistical package; and 2) complex segregation analysis implemented in the program package MAN. The effect of age and gender differences, gender hormones, as well as PTH and vitamin-D (calcidiol) plasma levels were evaluated simultaneously with the parameters of variance analysis. The results showed that about 50% of PICP variation is attributable to genetic factors. The effect of age was significant among men and postmenopausal women, whereas calcidiol influenced variation of PICP in premenopausal women. The results of variance analysis showed that some 40% of BGP, adjusted for confounding variables, can be explained in genetic factors. Age and PTH were important covariates for osteocalcin in men and premenopausal women. Exploration of the maximum likelihood estimates of the various hypotheses concerning the mode of intergenerational transmission of PICP and BGP demonstrated a good correspondence to the Mendelian mode of inheritance (i.e., major gene effect). 2000 Wiley-Liss, Inc.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11038447&dopt=Abstract
Cesk Patol. 1999 Apr;35(2):63-6.
[Papillary fibroelastoma of the endocardium]
[Article in Czech]
Kohout A.
Fingerlanduv ustav patologie, Hradec Kralove. kohoualnhk.cz
Six cases of papillary fibroelastoma of the endocardium were presented. All cases appeared as incidental findings at autopsy. Grossly, they were verrucous or tuft-like growths less than 1 cm in size on cardiac valves. Histologically, they consisted of a fibrocollagenous stalk and multiple papillary fronds with typical zonal architecture: central dense hyaline core containing elastic fibers surrounded by a layer of myxoid matrix and covered by hyperplastic endothelial cells. At the surface of papillary fronds there were foci of fibrin deposition. Histogenesis of papillary fibroelastomas is unclear, they are considered variously as primary benign tumours, hamartomas or organized thrombi.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11038657&dopt=Abstract
Zhonghua Yi Xue Za Zhi. 1998 Sep;78(9):699-701.
[Preventional intervention of myocardial interstitial fibrosis in murine myocardium with acute myocarditis]
[Article in Chinese]
Jing Z, Cheng X, Yang Y.
Division of Cardio-Pulmonary Circulation, Fuwai Heart Hospital & Institute of Cardiovascular Disease, PUMC & CAMS, Beijing.
OBJECTIVES: To explore that whether intervening the fibrosis of heart interstitium in acute viral myocarditis is practical or not, and offer the experimental basis for clinic to choose the optimum period to intervene myocardial fibrosis. METHODS: Animals were divided into three groups: myocarditis, myocarditis intervened by Losartan, and normal control. The death rate of every group was compared. HE staining and picrosirius red staining and circularly polarized light were used to investigate myocardial collagen expression. Cardiac output was measured by impedance differentiation, and cardiac index was computed to evaluate cardiac function. RESULTS: The death rate of the group with Losartan was 75.0%, and that of the myocarditis group was 41.7%. The cardiac index of the group with the drug was 0.014 +/- 0.001 ml.min-1.cm2, the myocarditis group 0.019 +/- 0.004 ml.min-1.cm2, and the normal control 0.024 +/- 0.002 ml.min-1.cm2. The scanning area of collagen in the group with the drug was 2.06 +/- 0.77 mm, the myocarditis group 4.72 +/- 2.22 mm and the normal control 3.74 +/- 1.50 mm. CONCLUSIONS: Collagen has increased in acute viral myocarditis, but its main role in this time is to repair the necrotic myocardium, and Losartan may block this process and make lesions develop. Therefore, the acute stage is not an practical period for intervening myocardial fibrosis in viral myocarditis.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11038797&dopt=Abstract
The average human scalp is covered by approximatey 100,000 hair follicles. Each hair undergoes
Loss of hair itself does not pose critical health problems because biological role of human hair is relatively marginal. Hair on our scalp protects the head from mechanical shock, heat loss, and exposure to UV-light. The eyelashes and eyebrowes protect the eyes, and hair in the ear canal or the nasal passages help filter out particles and pathogens, thus protecting our internal organs.
However, hair does play important social role: it is one of the major determinants of our appearance and identity in daily life. Fullness of hair also implicates or manifests physical integrity and youthfulness of the person. Losing hair could have more than just emotional impacts on individuals.
The hair is a unique organ that goes through a characteristic cycle consisting of an immature phase, a growing phase called anagen, a transitional phase between the growing phase and the resting phase called catagen, and finally a resting phase called telogen in which the hair stops growing, waiting to fall out. 85-90% of hairs on our body are in anagen phase or growing phase, which lasts anywhere from two to five years. This phase is followed by a short regression phase, or catagen, which lasts 2-3 weeks. Approximately 1% of hair follicles are in catagen. Approximately 10-15% of hair follicles are in the resting phase, the telogen, which lasts about 3-5 months. Hair follicles typically goes through 10-20 asynchronous cycles during the lifetime.
Persistent loss of more than 150 hairs would consist a state of hair loss, or alopecia, albeit it could be temporary.
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