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Mmp11  -  matrix metallopeptidase 11

Rattus norvegicus

Synonyms: MMP-11, Matrix metalloproteinase-11, SL-3, ST3, Stromelysin-3
 
 
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High impact information on Mmp11

  • Although the tissue distribution of the ST3 antigen was similar to that of Thy-1, it was not identical, and in the brain, the two structures were localized in different areas [1].
  • While none of the ST3, ST4 (fibroblast directed), or BN(MB)35 (myeloid directed) antibodies recognized fat cells cultured from marrow, the ST10 antibody, selected for binding to marrow derived fat cells, stained peripheral adipose cells, unidentified aglobular cells in areas of fat cell formation, and macrophages, but not fibroblasts [1].
  • Our results showed that in vitro incubation of macrophages with SA and SL3 antigens of A. suum did not result in NO release from cells, whereas incubation with ESA or ESL3 antigens resulted in the stimulation of NO production by these cells, both in a specific (inhibited by L-NAME and L-canavanine) and dose-dependent manner [2].
  • SUMMARY We investigated the in vitro effect of total excretory/secretory and somatic antigens from Ascaris suum adults (ESA and SA) and larvae 3 (ESL3 and SL3), and of 10 purified protein fractions from ESA components on rat alveolar macrophage nitric oxide (NO) production [2].
  • Biochemical determinations of non-collagenous protein and hydroxyproline were made on rat skeletal muscles following 7 days of space flight aboard the NASA space shuttle mission SL-3 [3].
 

Biological context of Mmp11

  • Also, the mitochondrial phosphorylation rate (PR), the respiratory control ratio (RC), and the state 3 respiration rate (ST 3) were significantly depressed to 62, 54, and 72% of the control values [4].
  • In addition mitochondrial function was preserved well: mitochondrial oxidative phosphorylation capacity remained at 94% of control levels, ST3 at 93%, and ADP/O at 100% of control [5].
  • A life science module housing young and mature rats was flown on shuttle mission Spacelab 3 (SL-3), and the results of hematology studies of flight and control rats are presented [6].
 

Anatomical context of Mmp11

  • Cyclic AMP-dependent protein kinase (cA-PK) activity was decreased in subcellular fractions of heart muscle of SL-3 animals [7].
  • Data from Spacelab 3 (SL3) suggested that spaceflight significantly reduces the activity of the rat tibial growth plate [8].
  • Protein kinase activity ratios were decreased in the soluble and increased in the particulate fractions of Spacelab 3 (SL-3) rat sublingual glands, compared with ground controls [9].
  • The specific activity of fatty acyl-CoA synthetase, which is responsible for activation of fatty acids, was 37% (P less than 0.05) higher in microsomes from the rats on SL-3; however, since these animals had 25% less microsomal protein (P less than 0.02), there was no difference per gram of liver [10].
  • Distribution changes of microtubules and cytoskeletal elements from both SL-3 and 1.7-G groups were observed [7].
 

Associations of Mmp11 with chemical compounds

  • Rechromatography of an eluate from this spot with another solvent system resolved it into three spots (SL1, SL2 and SL3, the mixture being designated as Substance L) which could be visualized either with iodine vapour, ninhydrin or molybdenum reagent [11].
  • The inclusion of rats aboard Spacelab 3 (SL-3) allowed analyses of liver lipids, glycogen, hepatic enzymes of cholesterol, glycerolipid and sphingolipid biosynthesis, and other enzyme activities [10].
  • The high Km cyclic AMP phosphodiesterase activity was lower (P less than 0.05) in SL-3 heart muscle, and low Km activity was lower in 1.7-G males but was unaltered in females [7].
 

Analytical, diagnostic and therapeutic context of Mmp11

  • Perfusion with insulin maintained a normal metabolic pattern: ATP 105%, TAN 97%, ECP 0.877, PR 94%, RC 69%, and ST 3 105% [4].

References

  1. Cellular composition of rat bone marrow stroma. Antigen-defined subpopulations. Sullivan, A.K., Claxton, D., Shematek, G., Wang, H. Lab. Invest. (1989) [Pubmed]
  2. Antigens from Ascaris suum trigger in vitro macrophage NO production. Andrade, M.A., Siles-Lucas, M., López-Abán, J., Carranza, C., Pérez-Arellano, J.L., Muro, A. Parasite Immunol. (2005) [Pubmed]
  3. Protein and collagen content of rat skeletal muscle following space flight. Martin, T.P. Cell Tissue Res. (1988) [Pubmed]
  4. Evaluation of a short-time, oxygen carrier-free perfusion model in rat liver: mitochondrial energy metabolism and insulin effect. Shimahara, Y., Isselhard, W. J. Surg. Res. (1986) [Pubmed]
  5. Studies of reperfusion injury in skeletal muscle: preserved cellular viability after extended periods of warm ischemia. Beyersdorf, F., Unger, A., Wildhirt, A., Kretzer, U., Deutschländer, N., Krüger, S., Matheis, G., Hanselmann, A., Zimmer, G., Satter, P. The Journal of cardiovascular surgery. (1991) [Pubmed]
  6. Hematological measurements in rats flown on Spacelab shuttle, SL-3. Lange, R.D., Andrews, R.B., Gibson, L.A., Congdon, C.C., Wright, P., Dunn, C.D., Jones, J.B. Am. J. Physiol. (1987) [Pubmed]
  7. Cardiac muscle ultrastructure and cyclic AMP reactions to altered gravity conditions. Mednieks, M.I., Fine, A.S., Oyama, J., Philpott, D.E. Am. J. Physiol. (1987) [Pubmed]
  8. The Spacelab 3 simulation: basis for a model of growth plate response in microgravity in the rat. Montufar-Solis, D., Duke, P.J., Morey-Holton, E. Journal of gravitational physiology : a journal of the International Society for Gravitational Physiology. (2001) [Pubmed]
  9. Salivary gland ultrastructure and cyclic AMP-dependent reactions in Spacelab 3 rats. Mednieks, M.I., Hand, A.R. Am. J. Physiol. (1987) [Pubmed]
  10. Hepatic function in rats after spaceflight: effects on lipids, glycogen, and enzymes. Merrill, A.H., Wang, E., Jones, D.P., Hargrove, J.L. Am. J. Physiol. (1987) [Pubmed]
  11. Separation and partial characterization of smooth muscle contractile material in the venom of the scorpion Heterometrus bengalensis. Kar, P.K., Sarangi, B., Datta, A., Gomes, A., Lahiri, S.C. Toxicon (1983) [Pubmed]
 
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