Differential expression of the C4 isozyme of lactate dehydrogenase (LDHC4) in developing bonefish (Albula sp.)

✍ Scribed by Pfeiler, Edward ;Vrijenhoek, Robert C.

• Publisher: John Wiley and Sons
• Year: 1988
• Tongue: English
• Weight: 406 KB
• Volume: 246
• Category: Article
• ISSN: 0022-104X
• DOI: 10.1002/jez.1402460313

✦ Synopsis

Starch-gel electrophoresis revealed that the C4 isozyme of lactate dehydrogenase (LDHC4) predominated in the gelatinous, postcranial body mass of metamorphosing leptocephalous larvae of the bonefish (Albula sp.), a primitive teleost fish. At the end of metamorphosis, when the juvenile stage was reached and the gelatinous matrix had been resorbed and replaced by muscle and bone, the relative activity of the C4 isozyme was reduced, and the expression of the A4 and B4 isozymes increased. The A4 isozyme then became the dominant form in white muscle of developing juveniles. The C4 isozyme was also expressed in juvenile eye, liver, heart, brain, gut, gill, and red muscle, but the B4 isozyme showed the highest relative activity in these tissues. These results suggest (1) that the Ldh-C gene is the most active of the three LDH genes in the leptocephalus, (2) that the C4 isozyme of LDH performs a critical and specific function in larval metabolism, and (3) that metamorphosis is accompanied by tissue-specific increases in activity of the Ldh-A and Ldh-B genes.

Lactate dehydrogenase (LDH; L-1actate:NAD ox-The presence of a leptocephalous larval stage in idoreductase; EC 1.1.1.27) is a tetrameric enzyme marine teleost fishes is considered a primitive trait that is encoded by three gene loci and (Greenwood et al., ,661, and thus we felt that a -C) in teleost fishes, birds, and mammals (Markert study of LDH isozyme patterns in developing et al., '75). Until recently, the commonly accepted bonefish would be of interest, given the current view concerning the evolutionary relationships of controversy over the evolution of LDH genes.