Disease relevance of LDHB

• These data demonstrate that LDH-B gene repression after hypoxia and reactivation after oxygen reperfusion occurs in both vascular and avascular retinal cells [1].

High impact information on LDHB

• Lactate dehydrogenase (LDH) isoenzymes, LDH-A and LDH-B, are expressed in premeiotic, meiotic cells, and early spermatids, both in avian and mammalian spermatogenesis [2].
• While mammals and columbid birds express the testis specific LDH-C gene in meiotic and postmeiotic cells, several LDH-B testis specific transcripts were detected in the corresponding cells during chicken spermatogenesis [2].
• In developing chick retina in situ hybridization localized LDH-B mRNA to aerobic regions of the retina, coincident with the distribution of active mitochondria [1].
• The three crystallins, alpha B-crystallin, tau-crystallin/alpha-enolase and epsilon-crystallin/lactate dehydrogenase B are all stress induced proteins and may thus share common regulatory elements [3].
• This species-specific difference may correlate with the difference in LDH-B activity between various chicken and duck tissues: the retina and pancreas in duck have significantly higher LDH-B activity than in chick, while heart, muscle, stomach, liver, intestine and kidney all have much higher LDH-B activity in chicken than in duck [3].

Anatomical context of LDHB

• These observations suggest that GB expressed only LDH-B and that GB cells are not lactate-producing cells, like astrocyte, but rather are lactate-consuming cells, similar to neurons in CNS [4].
• In the GB the subtype of LDH mRNA was LDM-B only, and in the cerebral cortex and spinal cord, the subtype of LDH mRNA was predominantly LDH-B, and a small amount of LDH-A was found in the chicken and embryo [4].

Analytical, diagnostic and therapeutic context of LDHB

• Northern and semi-quantitative RT/PCR analyses demonstrated that LDH-B mRNA levels decrease in primary rat and chick retinal cells in response to hypoxia [1].

References