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BCL2 CALM3 (1 - 2 of 2)
PMID: 11903930
Immunoreactivity for Bcl-2 and C-Jun/AP1 in hippocampal corpora amylacea after ischaemia in humans.
... and Bcl-2 within ... may cause the ... of CAm in ...   (details)

BCL2 CALM3

Type:  positive regulation
Is this interaction correct?
Yes
No

Comments

PMID: 11903930

Immunoreactivity for Bcl-2 and C-Jun/AP1 in hippocampal corpora amylacea after ischaemia in humans.
Source

Neuropathology and applied neurobiology (December 2001)

Abstract

Immunoreactivity for Bcl-2 and C-Jun/AP1 in hippocampal corpora amylacea after ischaemia in humans. Corpora amylacea (CAm) are regarded as a hallmark of brain ageing, but little is known about their role in normal and pathological circumstances. CAm contain, in addition to glucose polymers, ageing-, stress- and proinflammatory proteins. In view of their almost universal occurrence and their cumulation with time, formation of CAm may represent a basic mechanism for the management of metabolic degradation products. In this context, we studied samples from post-mortem cases with repetitive brain hypoxic episodes in the past history. We investigated, by immunohistochemistry, the presence of Bcl-2, c-jun and bax in CAm. CAm showed immunoreactivity for the mitochondrial membrane associated protein Bcl-2, and for the major component of activator protein 1 transcriptional factor c-Jun. We found higher numbers of CAm in the hippocampus and the dentate gyrus in cases with repetitive cerebral hypoxia than in controls. We conclude that: (1) the presence of C-Jun and Bcl-2 within the glucose polymer mass of CAm may be related to mitochondrial damage and/or a transient overload of proteolytic systems during cellular injury; and (2) repetitive cellular stress during life may cause the age-related increase of CAm in elderly subjects.

PMID: 17942410
A novel calmodulin-Ca2+ target recognition activates the Bcl-2 regulator FKBP38.
... and Bcl-2,... requires a ... sensor calmodulin (CaM).   (details)

BCL2 CALM3

Type:  positive regulation
Is this interaction correct?
Yes
No

Comments

PMID: 17942410

A novel calmodulin-Ca2+ target recognition activates the Bcl-2 regulator FKBP38.
Source

The Journal of biological chemistry (12/14/2007)

Abstract

A novel calmodulin-Ca2+ target recognition activates the Bcl-2 regulator FKBP38. The FK506-binding protein 38 (FKBP38) affects neuronal apoptosis control by suppressing the anti-apoptotic function of Bcl-2. The direct interaction between FKBP38 and Bcl-2, however, requires a prior activation of FKBP38 by the Ca2+ sensor calmodulin (CaM). Here we demonstrate for the first time that the formation of a complex between FKBP38 and CaM-Ca2+ involves two separate interaction sites, thus revealing a novel scenario of target protein regulation by CaM-Ca2+. The C-terminal FKBP38 residues Ser290-Asn313 bind to the target protein-binding cleft of the Ca2+-coordinated C-terminal CaM domain, thereby enabling the N-terminal CaM domain to interact with the catalytic domain of FKBP38 in a Ca2+-independent manner. Only the latter interaction between the catalytic FKBP38 domain and the N-terminal CaM domain activates FKBP38 and, as a consequence, also regulates Bcl-2.