Characterization of the single peptide generated from the amino-terminus end of α- and β-hemoglobin chains by the Ca2+-dependent neutral proteinase

Melloni, Edon; Salamino, Franca; Sparatore, Bianca; Michetti, M.; Pontremoli, S.

doi:10.1016/0167-4838(84)90291-7

Cited by 24 publications

(5 citation statements)

References 10 publications

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“…For instance, Ca2+-dependent neutral proteases present in human erythrocytes degrade the membrane proteins designated band 2.1 and 4.1 but do not act on other proteins (Pontremoli et al, 1984). This differential sensitivity appears to be due to a requirement for specific sequences that can be cleaved by the enzymes (Melloni et al, 1984). Even the very active lysosomal proteases show some selectivity.…”

Section: Susceptibility To Pre-golgi Degradation Is An Inherent Property Of Each Tcr Subunitmentioning

confidence: 99%

Pre-Golgi degradation of newly synthesized T-cell antigen receptor chains: intrinsic sensitivity and the role of subunit assembly.

Bonifacino

Suzuki

Lippincott‐Schwartz

et al. 1989

The Journal of Cell Biology

220

141

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Abstract. The T cell antigen receptor (TCR) is a multisubunit complex composed of at least seven transmembrane chains. The predominant species in most T cells has the composition otfly6~2. The roles of subunit assembly in transport out of the ER and in the recently described process of pre-Golgi degradation of newly synthesized TCR chains were analyzed in a T-cell line deficient in the synthesis of fi chains (A2) and in COS-1 fibroblasts transfected with genes encoding individual TCR chains. Studies with the fi-deficient T-cell line showed that, in the absence of fi, the other TCR chains were synthesized at normal rates, but, instead of being transported to the cell surface, they were retained in the ER. Analysis of the fate of TCR chains retained in the ER showed that they were degraded at vastly different rates by a nonlysosomal pathway. Whereas the t~ chains were degraded rapidly, 3;, ~', and e were relatively long-lived. To analyze whether this selective degradation was because of different intrinsic susceptibility of the individual chains to degradation or to the formation of resistant oligomers, TCR chains were expressed alone or in combinations in COS-1 fibroblasts. These studies showed that (a) individual TCR chains were degraded at different rates when expressed alone in COS-1 cells, and (b) sensitive chains could be stabilized by coexpression with a resistant chain. Taken together, these observations indicate that both intrinsic sensitivity and subunit assembly play a role in determining the rates at which newly synthesized TCR chains are degraded in the ER.

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Section: Susceptibility To Pre-golgi Degradation Is An Inherent Property Of Each Tcr Subunitmentioning

confidence: 99%

Pre-Golgi degradation of newly synthesized T-cell antigen receptor chains: intrinsic sensitivity and the role of subunit assembly.

Bonifacino

Suzuki

Lippincott‐Schwartz

et al. 1989

The Journal of Cell Biology

220

141

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“…Myogenic transcription factors could positively regulate this activity. On the other hand calpain activity could be also negatively regulated by phosphorylation through PKA or its endogenous inhibitor calpastatin (Melloni et al, 1984;Inomata et al, 1988;Saido et al, 1992;Croall and McGrody, 1994;Moldoveanu et al, 2001;Shiraha et al, 2002;Dedieu et al, 2003(a)). The calpain family is thought to be involved in a range of various diseases such as cataract formation, diabetes, rheumatoid arthritis, ischemia, neurodegenerative diseases and muscular dystrophies (David et al, 1993;Saito et al, 1993;Mouatt-Prigent et al, 1996;Hirsch et al, 1997;Ishikawa et al, 1999;Horikawa et al, 2000;Richard et al, 2000;Tidball and Spencer 2000;Tamada et al, 2001;Trumbeckaite et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Myoblast migration is prevented by a calpain‐dependent accumulation of MARCKS

Dedieu

Mazères

Poussard

et al. 2003

Biology of the Cell

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Calpains, also called calcium activated neutral cysteine proteases are presently known to play pivotal roles in physiological and biological phenomena such as signal transduction, cell spreading and motility, apoptosis, regulation of cell cycle and regulation of muscle cell differentiation. Concerning this last point, calpains have been shown to play a crucial role during the earlier myogenesis. In this study we have analyzed the involvement of calpains during an important step of myogenesis: myoblast migration. Our findings show that myoblast migration was drastically reduced when the expression of µ-and m-calpain was decreased. We have also observed that MARCKS (myristoylated alanine rich C kinase substrate), a protein localized at focal adhesion sites, was significantly accumulated when the expression levels of calpains were decreased. Also, using phorbol myristate acetate, (an activator of PKC) and plasmids carrying the full-length cDNA of MARCKS or a cDNA fragment lacking the phosphorylation site domain, we demonstrated that normal myoblast migration is dependent on MARCKS phosphorylation and localization.

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“…It should be noted that only μ-calpain has been detected in human erythrocytes [32]. Previous work has demonstrated that erythrocyte μ-calpain is not only involved in the degradation of submembranous cytoskeleton proteins but also utilizes native as well as heme-deprived α- and β-globin chains as substrate [33].…”

Section: Discussionmentioning

confidence: 98%

Clinical Severity of β-thalassaemia/Hb E Disease Is Associated with Differential Activities of the Calpain-Calpastatin Proteolytic System

et al. 2012

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Earlier observations in the literature suggest that proteolytic degradation of excess unmatched α-globin chains reduces their accumulation and precipitation in β-thalassaemia erythroid precursor cells and have linked this proteolytic degradation to the activity of calpain protease. The aim of this study was to correlate the activity of calpain and its inhibitor, calpastatin, with different degrees of disease severity in β-thalassaemia. CD34+ cells were enriched from peripheral blood of healthy individuals (control group) and patients with mild and severe clinical presentations of β0-thalassaemia/Hb E disease. By ex vivo cultivation promoting erythroid cell differentiation for 7 days, proerythroblasts, were employed for the functional characterization of the calpain-calpastatin proteolytic system. In comparison to the control group, enzymatic activity and protein amounts of μ-calpain were found to be more than 3-fold increased in proerythroblasts from patients with mild clinical symptoms, whereas no significant difference was observed in patients with severe clinical symptoms. Furthermore, a 1.6-fold decrease of calpastatin activity and 3.2-fold accumulation of a 34 kDa calpain-mediated degradation product of calpastatin were observed in patients with mild clinical symptoms. The increased activity of calpain may be involved in the removal of excess α-globin chains contributing to a lower degree of disease severity in patients with mild clinical symptoms.

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Characterization of the single peptide generated from the amino-terminus end of α- and β-hemoglobin chains by the Ca2+-dependent neutral proteinase

Cited by 24 publications

References 10 publications

Pre-Golgi degradation of newly synthesized T-cell antigen receptor chains: intrinsic sensitivity and the role of subunit assembly.

Pre-Golgi degradation of newly synthesized T-cell antigen receptor chains: intrinsic sensitivity and the role of subunit assembly.

Myoblast migration is prevented by a calpain‐dependent accumulation of MARCKS

Clinical Severity of β-thalassaemia/Hb E Disease Is Associated with Differential Activities of the Calpain-Calpastatin Proteolytic System

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