Disease relevance of Kap

• Apparently no such correlation exists between binding constants (Kap M-1)-10-4) of DNA (6.4--11.2) and of chromatin (3.1--8.3), but Kap M-1 of chromatin isolated from mouse fibrosarcoma and Yoshida ascites sarcoma are 1.5--3 times higher than that found for mouse and rat liver chromatin [1].

High impact information on Kap

• Immunostaining using anti-alpha KAP antibodies suggests that alpha KAP is associated with sarcomeres of skeletal muscle fibers [2].
• Analysis of the exon-intron structure revealed that the alpha KAP transcript is derived from the alpha CaMKII gene by alternative promoter usage and RNA splicing [2].
• The temporal pattern of expression of KAP in the uterus closely overlapped with the profile of plasma estrogen during pregnancy [3].
• Estrogen regulates the stage-specific expression of kidney androgen-regulated protein in rat uterus during reproductive cycle and pregnancy [3].
• Known antagonists of estrogen, such as tamoxifen and ICI 182,780, strongly inhibited uterine KAP gene expression during the estrous cycle and pregnancy, supporting a regulatory role of estrogen in this process [3].

Biological context of Kap

• Our results showed a high level of KAP messenger RNA (mRNA) in the uteri of nonpregnant rats at all stages of the estrous cycle [3].
• Treatment of these animals with progesterone, on the other hand, did not significantly after KAP gene expression [3].
• Interestingly, the level of KAP mRNA started to rise again toward the end (day 19 onward) of pregnancy and was high during parturition [3].
• Our studies, therefore, revealed that KAP is a useful marker of estrogen action in the uterus, especially during the reproductive cycle and termination of gestation [3].
• That raises the question of whether CaM K II-mediated phosphorylation of alpha KAP and triadin together might be involved in a molecular signaling pathway important for SR Ca(2+)-release in fast-twitch muscle SR [4].

Anatomical context of Kap

• Immunocytochemical analyses of uterine sections with an antibody against KAP exhibited specific staining in both luminal and glandular epithelia and in myometrium [3].
• Recently, it was shown that RNA splicing of brain-specific alpha CaM K II, gives rise to a truncated protein (alpha KAP), consisting mainly of the association domain, serving to anchor CaM K II to SR membrane in rat skeletal muscle [Bayer, K.-U., et al. (1998) EMBO J. 19, 5598-5605] [4].

Associations of Kap with chemical compounds

• Glucose consumption and Kap value were then compared [5].
• This gene encodes the previously identified androgen-regulated protein known as the kidney androgen-regulated protein (KAP) because of its abundant expression in the kidney [3].
• In the present study, we searched for the presence of alpha KAP in sucrose-density purified SR membrane fractions from representative fast-twitch and slow-twitch limb muscles, both of the rabbit and the rat, using immunoblot techniques and antibody directed against the association domain of alpha CaM K II [4].

Analytical, diagnostic and therapeutic context of Kap

• Putative alpha KAP was immunodetected as a 23-kDa electrophoretic component on SDS-PAGE of the isolated SR from fast-twitch but not from slow-twitch muscle, and was further identified as a specific substrate of endogenous CaM K II, in the rabbit [4].
• Northern blot analysis with a probe specific for alpha KAP detected three distinct mRNA species of 4.0, 2.4, and 1.5 kb in rat skeletal muscle [6].

References