Literature DB >> 9889261

Presence in human skeletal muscle of an AMP deaminase-associated protein that reacts with an antibody to human plasma histidine-proline-rich glycoprotein.

A R Sabbatini1, M Ranieri-Raggi, L Pollina, P Viacava, J R Ashby, A J Moir, A Raggi.   

Abstract

Histidine-proline-rich glycoprotein (HPRG) is a protein that is synthesized by parenchimal liver cells. The protein has been implicated in a number of plasma-specific processes, including blood coagulation and fibrinolysis. We have recently reported the association of an HPRG-like protein with rabbit skeletal muscle AMP deaminase (AMPD). The results of the immunological analysis reported here demonstrate that an antibody against human plasma HPRG reacts with an AMPD preparation from human skeletal muscle. To probe the localization of the putative HPRG-like protein in human skeletal muscle, serial sections from frozen biopsy specimens were processed for immunohistochemical and histoenzymatic stains. A selective binding of the anti-HPRG antibody to Type IIB muscle fibers was detected, suggesting a preferential association of the novel protein to the AMPD isoenzyme contained in the fast-twitch glycolytic fibers.

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Year:  1999        PMID: 9889261     DOI: 10.1177/002215549904700214

Source DB:  PubMed          Journal:  J Histochem Cytochem        ISSN: 0022-1554            Impact factor:   2.479


  7 in total

1.  Immunohistochemical localization of histidine-rich glycoprotein in human skeletal muscle: preferential distribution of the protein at the sarcomeric I-band.

Authors:  L Mattii; L Rossi; C Ippolito; G Alì; D Martini; A Raggi; Antonietta R M Sabbatini
Journal:  Histochem Cell Biol       Date:  2017-07-12       Impact factor: 4.304

2.  In focus in HCB.

Authors:  Douglas J Taatjes; Jürgen Roth
Journal:  Histochem Cell Biol       Date:  2017-11-09       Impact factor: 4.304

3.  Immunohistochemical analysis of human skeletal muscle AMP deaminase deficiency. Evidence of a correlation between the muscle HPRG content and the level of the residual AMP deaminase activity.

Authors:  Antonietta R M Sabbatini; Antonio Toscano; Mohammed Aguennouz; Daniela Martini; Enza Polizzi; Maria Ranieri-Raggi; Arthur J G Moir; Alba Migliorato; Olimpia Musumeci; Giuseppe Vita; Antonio Raggi
Journal:  J Muscle Res Cell Motil       Date:  2006-03-29       Impact factor: 2.698

4.  Ultrastructural Localization of Histidine-rich Glycoprotein in Skeletal Muscle Fibers: Colocalization With AMP Deaminase.

Authors:  Letizia Mattii; Francesco Bianchi; Alessandra Falleni; Sabina Frascarelli; Matilde Masini; Greta Alì; Grazia Chiellini; Antonietta R M Sabbatini
Journal:  J Histochem Cytochem       Date:  2019-12-27       Impact factor: 2.479

5.  Evidence that muscle cells do not express the histidine-rich glycoprotein associated with AMP deaminase but can internalise the plasma protein.

Authors:  A R M Sabbatini; L Mattii; B Battolla; E Polizzi; D Martini; M Ranieri-Raggi; A J G Moir; A Raggi
Journal:  Eur J Histochem       Date:  2011-02-25       Impact factor: 3.188

Review 6.  The role of histidine-proline-rich glycoprotein as zinc chaperone for skeletal muscle AMP deaminase.

Authors:  Maria Ranieri-Raggi; Arthur J G Moir; Antonio Raggi
Journal:  Biomolecules       Date:  2014-05-05

Review 7.  Role of the HPRG Component of Striated Muscle AMP Deaminase in the Stability and Cellular Behaviour of the Enzyme.

Authors:  Francesca Ronca; Antonio Raggi
Journal:  Biomolecules       Date:  2018-08-23
  7 in total

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