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Cell Mol Biol (Noisy-le-grand). 2000 Nov;46(7):1219-25.
Original method for the histochemical demonstration of tripeptidyl aminopeptidase I.

Dikov A, Dimitrova M, Ivanov I, Krieg R, Halbhub KJ.

Institute of Experimental Morphology and Anthropology, Bulgarian Academy of Sciences, Sofia.

The original histochemical method for the visualization of tripeptidyl aminopeptidase I (TPP I, EC 3.4.14.9) is developed. The method is based on the new synthetic substrates Gly-L-Pro-L-Met(or L-Ala)-5-chloro-1-anthraquinonyl hydrazide (Gly-Pro-Met[Ala]-CAH). The final reaction product is represented as tripeptidyl-5-chloro-1 anthraquinonyl hydrazides (TPP-CAH). Upon the enzyme action the practically in aqueous media insoluble brown-reddish dye 5-chloro-1-anthraquinonyl hydrazine (CAH) is released, which reacts simultaneously with aromatic aldehydes as e.g. 4-anisaldehyde (p-AA) or 4-nitrobenzaldehyde (p-NBA), resulting in microcrystalline or amorphous deeply colored hydrazones. The last compounds mark accurately the locations of enzymatic activity. The biochemically suggested lysosomal localization of this collagen-degrading exopeptidase is thus confirmed on tissue sections. More information about the distribution of TPP I in different rat organs is presented as well.


online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11075951&dopt=Abstract



Pancreas. 2000 Nov;21(4):358-68.
Establishment of human pancreatic ductal cells in a long-term culture.

Ulrich AB, Schmied BM, Matsuzaki H, El-Metwally T, Moyer MP, Ricordi C, Adrian TE, Batra SK, Pour PM.

UNMC Eppley Cancer Center, Omaha 68198-6805, USA.

Cultivation and preservation of human pancreatic ductal cells have remained a challenge. With a defined culture medium and refinement of culturing techniques, we have been able to maintain human pancreatic ductal cells without any genetic manipulation in culture for more than 16 months. Freshly isolated ductal fragments were placed on a rocker in M3:5 medium free of collagen for 14 days to remove fibroblasts and endocrine cells before allowing them to attach. The cells produced an excessive amount of mucin and expressed the duct specific cytokeratins (CK) 7 and 19, DU-PAN2, CA19-9, carbonic anhydrase II (CA II), and secretin receptors. During the course of the culture, however, the cells gradually lost the expression of CA II, secretin receptors, DU-PAN2, and CA 19-9 and assumed an undifferentiated phenotype, which showed an upregulation of transforming growth factor alpha (TGFalpha) and epidermal growth factor receptor (EGFR), an increase in the expression of Ki-67, and an increased binding to Phaseolus vulgaris leucoagglutinin (PHA-L) and tomato lectin. These ductal cells present a useful source with which to study physiologic aspects of ductal cells including differentiation.


online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11075990&dopt=Abstract



Development. 2000 Dec;127(24):5475-85.
Papilin in development; a pericellular protein with a homology to the ADAMTS metalloproteinases.

Kramerova IA, Kawaguchi N, Fessler LI, Nelson RE, Chen Y, Kramerov AA, Kusche-Gullberg M, Kramer JM, Ackley BD, Sieron AL, Prockop DJ, Fessler JH.

MCD Biology Department and Molecular Biology Institute, University of California at Los Angeles, CA 90095, USA.

Papilin is an extracellular matrix glycoprotein that we have found to be involved in, (1) thin matrix layers during gastrulation, (2) matrix associated with wandering, phagocytic hemocytes, (3) basement membranes and (4) space-filling matrix during Drosophila development. Determination of its cDNA sequence led to the identification of Caenorhabditis and mammalian papilins. A distinctly conserved 'papilin cassette' of domains at the amino-end of papilins is also the carboxyl-end of the ADAMTS subgroup of secreted, matrix-associated metalloproteinases; this cassette contains one thrombospondin type 1 (TSR) domain, a specific cysteine-rich domain and several partial TSR domains. In vitro, papilin non-competitively inhibits procollagen N-proteinase, an ADAMTS metalloproteinase. Inhibiting papilin synthesis in Drosophila or Caenorhabditis causes defective cell arrangements and embryonic death. Ectopic expression of papilin in Drosophila causes lethal abnormalities in muscle, Malpighian tubule and trachea formation. We suggest that papilin influences cell rearrangements and may modulate metalloproteinases during organogenesis.


online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11076767&dopt=Abstract



J Cell Biol. 2000 Nov 13;151(4):779-88.
Differential expression of lumican and fibromodulin regulate collagen fibrillogenesis in developing mouse tendons.

Ezura Y, Chakravarti S, Oldberg A, Chervoneva I, Birk DE.

Department of Pathology Anatomy and Cell Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.

Collagen fibrillogenesis is finely regulated during development of tissue-specific extracellular matrices. The role(s) of a leucine-rich repeat protein subfamily in the regulation of fibrillogenesis during tendon development were defined. Lumican-, fibromodulin-, and double-deficient mice demonstrated disruptions in fibrillogenesis. With development, the amount of lumican decreases to barely detectable levels while fibromodulin increases significantly, and these changing patterns may regulate this process. Electron microscopic analysis demonstrated structural abnormalities in the fibrils and alterations in the progression through different assembly steps. In lumican-deficient tendons, alterations were observed early and the mature tendon was nearly normal. Fibromodulin-deficient tendons were comparable with the lumican-null in early developmental periods and acquired a severe phenotype by maturation. The double-deficient mice had a phenotype that was additive early and comparable with the fibromodulin-deficient mice at maturation. Therefore, lumican and fibromodulin both influence initial assembly of intermediates and the entry into fibril growth, while fibromodulin facilitates the progression through growth steps leading to mature fibrils. The observed increased ratio of fibromodulin to lumican and a competition for the same binding site could mediate these transitions. These studies indicate that lumican and fibromodulin have different developmental stage and leucine-rich repeat protein specific functions in the regulation of fibrillogenesis.


online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11076963&dopt=Abstract



J Cell Biol. 2000 Nov 13;151(4):879-89.
Matrix metalloproteinase 9 and vascular endothelial growth factor are essential for osteoclast recruitment into developing long bones.

Engsig MT, Chen QJ, Vu TH, Pedersen AC, Therkidsen B, Lund LR, Henriksen K, Lenhard T, Foged NT, Werb Z, Delaisse JM.

OSTEOPRO A/S and Center for Clinical and Basic Research, DK-2750 Herlev/Ballerup, Denmark. msteopro.dk

Bone development requires the recruitment of osteoclast precursors from surrounding mesenchyme, thereby allowing the key events of bone growth such as marrow cavity formation, capillary invasion, and matrix remodeling. We demonstrate that mice deficient in gelatinase B/matrix metalloproteinase (MMP)-9 exhibit a delay in osteoclast recruitment. Histological analysis and specialized invasion and bone resorption models show that MMP-9 is specifically required for the invasion of osteoclasts and endothelial cells into the discontinuously mineralized hypertrophic cartilage that fills the core of the diaphysis. However, MMPs other than MMP-9 are required for the passage of the cells through unmineralized type I collagen of the nascent bone collar, and play a role in resorption of mineralized matrix. MMP-9 stimulates the solubilization of unmineralized cartilage by MMP-13, a collagenase highly expressed in hypertrophic cartilage before osteoclast invasion. Hypertrophic cartilage also expresses vascular endothelial growth factor (VEGF), which binds to extracellular matrix and is made bioavailable by MMP-9 (Bergers, G., R. Brekken, G. McMahon, T.H. Vu, T. Itoh, K. Tamaki, K. Tanzawa, P. Thorpe, S. Itohara, Z. Werb, and D. Hanahan. 2000. Nat. Cell Biol. 2:737-744). We show that VEGF is a chemoattractant for osteoclasts. Moreover, invasion of osteoclasts into the hypertrophic cartilage requires VEGF because it is inhibited by blocking VEGF function. These observations identify specific actions of MMP-9 and VEGF that are critical for early bone development.


online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11076971&dopt=Abstract







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