Disease relevance of PRM3

• Hence, the ability of Prm3 and a series of Prm3 deleted/mutated subfragments to direct reporter gene expression in human erythroleukemia 92.1.7 and human embryonic kidney 293 cells was investigated [1].

High impact information on PRM3

• Previous studies established that 15d-Delta12,14-prostaglandin J2 (15d-PGJ2) selectively inhibits Prm3 activity and TPbeta expression through a peroxisome proliferator-activated receptor (PPAR)gamma mechanism without affecting Prm1 activity or TPalpha expression in human megakaryocytic erythroleukemia (HEL) 92.1.7 cells [2].
• Furthermore, the binary (activator) complex formed between PG and SAK mutant, PRM3, lacking the N-terminal lysine 11, exhibited 3-4-fold reduced binding with PG, Pm or miniplasmin substrate during ternary complex formation as compared to native SAK [3].
• The results show that human protamine 3 elutes first, closely followed by protamine 2 [4].
• The aim of the current study was to determine the key factors regulating TPbeta expression by functionally characterizing Prm3, identifying the core promoter and the cis-acting elements regulating basal Prm3 activity [1].
• Moreover, herein it was established that the core AP-1 element mediates phorbol myristic acid-induction of Prm3 activity hence providing a mechanistic explanation of phorbol ester up-regulation of TPbeta mRNA expression [1].

Biological context of PRM3

• Furthermore, three distinct regulatory regions comprising of an upstream repressor sequence, located between -404 to -320, and two positive regulatory regions required for efficient basal gene expression, located between -154 to -106 and -50 to +1, were identified within the core Prm3 [1].

Anatomical context of PRM3

• Protamine 3 mg . Kg-1 was injected over 30 sec. intravenously in the IV group (n = 5) and into the ascending aorta in the IA group (n = 5) [5].

Other interactions of PRM3

• Analysis described here supports the view that a fourth candidate coding region, gene4/Prm3, was derived from PRM1 during the genesis of the PRM1-->PRM2-->TNP2 domain [6].

Analytical, diagnostic and therapeutic context of PRM3

• Deletion and site-directed mutagenesis of consensus Oct-1/2 and AP-1 elements within the latter -154 to -106 and -50 to +1 regions, respectively, substantially reduced Prm3 activity while mutation of both elements abolished Prm3 activity [1].

References