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Gene Review

CAPN2  -  calpain 2, (m/II) large subunit

Sus scrofa

 
 
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Disease relevance of CAPN2

  • When YT-C3 cell, which is an uninfected, natural killer-like cell, was transfected with HTLV-I gene, the resulting transformed stable cells, YT-4 and YT-5.1, were found to produce increased amounts of calpain II concomitant with that of interleukin (IL)-2 receptor protein [1].
  • By contrast, only nine cell-line cells were positive in calpain II, and they were, without exception, the lineage which had been infected with HTLV-I, the retrovirus responsible for human adult T-cell leukemia [1].
 

High impact information on CAPN2

 

Biological context of CAPN2

 

Anatomical context of CAPN2

  • In the present study, we have examined the possibility that a Ca2+-activated, neutral protease, calpain II, may be associated with sperm membranes [5].
  • The proximity of calpain II to the acrosome suggests a potential role for the protease in the Ca2+-mediation of the acrosome reaction [5].
  • Calpain I, a low-Ca2 +-requiring form from porcine and human erythrocytes, and calpain II, a high-Ca2 +-requiring form from porcine kidney, were separated into their respective 80K and 30K subunits by high-performance liquid chromatography on a TSK-Gel G3000SW column in 1 M NaSCN [6].
  • The enhanced production of calpain II in HTLV-I infected T-cells was also confirmed by running chromatographic analyses on the homogenates of these cells, and comparing them with those of uninfected T-cells [1].
 

Associations of CAPN2 with chemical compounds

  • The hyaluronic acid-binding region was lost from the major glycosaminoglycan-bearing region after incubation with calpain II [7].
  • 1. Four calpain II heterodimers (80 kDa/30 kDa, 80 kDa/29 kDa, 80 kDa/26 kDa and 80 kDa/18 kDa) were isolated from fresh porcine kidney by (NH4)2SO4 precipitation, chromatography on DEAE-Sepharose CL-6B and subsequently on Reactive Red 120/agarose followed by f.p.l.c. on a Q-Sepharose Hi-Load 16/10 column [4].
  • 2. The major component (80 kDa/30 kDa) was used to provide the catalytically active calpain II 80 kDa/18 kDa heterodimer by treatment with CaCl2; titration with trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane (E64) in the presence of monothioglycerol showed the preparation to have 1.0 +/- 0.05 catalytic sites per molecule of heterodimer [4].
  • Amidase-like activity of calpain I and calpain II on substance P and its related peptides [8].
  • Porcine calpain II (Ca2+-dependent cysteine proteinase) was found to cleave human von Willebrand Factor (HvWF) into two major fragments (approximately 165 kDa and 145 kDa) in sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis (PAGE) [9].
 

Regulatory relationships of CAPN2

 

Other interactions of CAPN2

  • Two forms of Ca2+-dependent cysteine proteinase (calpain, EC 3.4.22.17) and their specific endogenous inhibitor (calpastatin) were partially purified from porcine retina: calpain I (low-Ca2+-requiring form) was half-maximally activated at 8 microM-Ca2+, and calpain II (high-Ca2+-requiring form) at 250 microM-Ca2+ [10].
 

Analytical, diagnostic and therapeutic context of CAPN2

  • Microinjection of calpain II near the nucleus of a PtK1 cell promoted the onset of metaphase [2].
  • To examine the possible involvement of a ubiquitous Ca2+-activated protease, calpain II, in the mitotic process, synchronized PtK1 cells were monitored by immunofluorescence for the relocation of calpain II [2].
  • Apparent immunological cross-reactivity between the larger subunits of calpain I (low Ca2+-requiring form) and calpain II (high Ca2+-requiring form) was calculated to be 15-17%, and two steps of affinity chromatography were needed to obtain antibodies which can discriminate between the two proteases [11].
  • Using indirect immunofluorescence with primary antibodies, which are polyclonal and monoclonal antibodies directed against the 80 kDa subunit of calpain II, we have established the presence of this antigen in porcine sperm [5].
  • Mono-specific antibodies directed toward the respective large and small subunits were used for immunoblotting experiments which established not only the identity among several porcine tissues of calpain I but also that of calpain II. several porcine tissues of calpain I but also that of calpain II [12].

References

  1. Gene expression for calpain isozymes in human hematopoietic system cells. Murachi, T., Adachi, Y., Hatanaka, M., Ishihara, G., Takano, E., Yamagata, Y., Kannagi, R. Prog. Clin. Biol. Res. (1990) [Pubmed]
  2. Calpain II involvement in mitosis. Schollmeyer, J.E. Science (1988) [Pubmed]
  3. Calcium-dependent proteinases and specific inhibitors: calpain and calpastatin. Murachi, T. Biochem. Soc. Symp. (1984) [Pubmed]
  4. Catalytic-site characteristics of the porcine calpain II 80 kDa/18 kDa heterodimer revealed by selective reaction of its essential thiol group with two-hydronic-state time-dependent inhibitors: evidence for a catalytic site Cys/His interactive system and an ionizing modulatory group. Mellor, G.W., Sreedharan, S.K., Kowlessur, D., Thomas, E.W., Brocklehurst, K. Biochem. J. (1993) [Pubmed]
  5. Identification of calpain II in porcine sperm. Schollmeyer, J.E. Biol. Reprod. (1986) [Pubmed]
  6. Reconstitution of calpain I and calpain II from their subunits: interchangeability of the light subunits. Kikuchi, T., Yumoto, N., Sasaki, T., Murachi, T. Arch. Biochem. Biophys. (1984) [Pubmed]
  7. Characterization of proteoglycan degradation by calpain. Suzuki, K., Shimizu, K., Hamamoto, T., Nakagawa, Y., Murachi, T., Yamamuro, T. Biochem. J. (1992) [Pubmed]
  8. Amidase-like activity of calpain I and calpain II on substance P and its related peptides. Hatanaka, M., Sasaki, T., Kikuchi, T., Murachi, T. Arch. Biochem. Biophys. (1985) [Pubmed]
  9. Amino acid analysis of human von Willebrand factor fragments cleaved by porcine calpain II. Nozaki, H. Tokai J. Exp. Clin. Med. (1987) [Pubmed]
  10. Calpain and calpastatin in porcine retina. Identification and action on microtubule-associated proteins. Yoshimura, N., Tsukahara, I., Murachi, T. Biochem. J. (1984) [Pubmed]
  11. Intracellular localization of two distinct Ca2+-proteases (calpain I and calpain II) as demonstrated by using discriminative antibodies. Yoshimura, N., Hatanaka, M., Kitahara, A., Kawaguchi, N., Murachi, T. J. Biol. Chem. (1984) [Pubmed]
  12. Large-scale purification of porcine calpain I and calpain II and comparison of proteolytic fragments of their subunits. Kitahara, A., Sasaki, T., Kikuchi, T., Yumoto, N., Yoshimura, N., Hatanaka, M., Murachi, T. J. Biochem. (1984) [Pubmed]
 
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