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Sequences and expression patterns of alkaline phosphatase isozymes in preattachment bovine embryos and the adult bovine
Author(s) -
McDougall K.,
Beecroft J.,
Wasnidge C.,
King W.A.,
Hahnel A.
Publication year - 1998
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/(sici)1098-2795(199805)50:1<7::aid-mrd2>3.0.co;2-p
Subject(s) - biology , isozyme , embryo , microbiology and biotechnology , gene expression , alkaline phosphatase , reverse transcription polymerase chain reaction , embryogenesis , messenger rna , bovine genome , embryonic stem cell , gene , genetics , enzyme , biochemistry , genome
We report the cloning and partial sequences of two novel bovine tissue‐specific alkaline phosphatase (AP) isozymes (TSAP2 and TSAP3) from in vitro–produced bovine blastocysts. Using a reverse‐transcribed polymerase chain reaction (RT‐PCR)–based assay for mRNA expression and in vitro–produced preattachment bovine embryos, TSAP2 mRNA was detected first at the four‐cell stage prior to the major burst of embryonic transcription in cattle and TSAP3 at the eight‐cell stage with the major burst in transcription. Furthermore, the transcription of TSAP2 and TSAP3 displays a curious “on‐off” pattern during early cleavages between 40 and 120 hr after insemination. Activity of bovine AP, measured by an azo‐dye coupling technique, indicates that at least one AP isozyme is functional in oocytes and embryos throughout bovine preattachment development. However, maternal and embryonic‐derived AP activity may have different cell‐surface distributions. This novel expression pattern of the bovine AP isozymes could provide a useful tool for identifying and clarifying the events controlling transcription and gene expression during early embryo development. Mol. Reprod. Dev. 50:7–17, 1998. © 1998 Wiley‐Liss, Inc.