A positive association between HBP levels and ETS exposure was confirmed. HBP measurement is recommended in population-based studies investigating the effects of ETS exposure. ETS exposure may increase BP, thereby synergistically contributing to unfavorable cardiovascular outcomes along with other deleterious effects of ETS.

Abstract.A high cyclic adenosine monophosphate (cAMP) level in fully-grown immature oocytes prevents meiotic resumption. In Xenopus, inhibitory cAMP is synthesized within oocytes depending on a stimulatory α-subunit of G-protein (Gsα). In the present study, we examined whether ooplasmic Gsα is involved in meiotic arrest of porcine oocytes. First, we studied the presence of Gsα molecules in porcine oocytes by immunoblotting, and this suggested the presence of reported isoforms (45 and 48 kDa) not only in cumulus cells but also in porcine oocytes. Then we injected an anti-Gsα antibody into porcine immature oocytes and found that inhibition of ooplasmic Gsα functions significantly promoted germinal vesicle breakdown of the oocytes, whose spontaneous meiotic resumption was prevented by 3-isobutyl-l-methylxanthine (IBMX) treatment. Although cyclin B synthesis and Mphase promoting factor (MPF) activation were largely prevented until 30 h of culture in IBMX-treated oocytes, injection of anti-Gsα antibody into these oocytes partially recovered cyclin B synthesis and activated MPF activity at 30 h. These results suggest that meiotic resumption of porcine oocytes is prevented by ooplasmic Gsα, which may stimulate cAMP synthesis within porcine oocytes, and that synthesized cAMP prevents meiotic resumption of oocytes through the signaling pathways involved in MPF activation.

Whey acidic protein (WAP) has been identified as a major whey protein in milk of a wide range of species and reportedly plays important roles in regulating the proliferation of mammary epithelial cells. However, in some species including humans, WAP is not synthesized in the mammary gland. The presence of WAP in carnivore species has not been reported. We searched the National Center for Biotechnology Information (NCBI) database for the dog WAP gene and tried biochemically to identify WAP in dog milk. The nucleotide sequence of the examined dog genomic DNA was completely identical to that in the NCBI database and showed that the dog WAP gene, like other known functional WAP genes, has four exons. Whey acidic protein (WAP) has been identified in various species as a major whey protein in milk [1, 3-6, 9, 15, 21]. WAPs share structural similarity with serine protease inhibitors containing WAP motif domains characterized by a four-disulfide core (4-DSC) [9]. Possible physiological functions of WAP have been proposed based on its similarity to protease inhibitor [6]. Our previous studies on WAP function utilizing in vivo [7,10,12,16] and in vitro [11,16,19] systems showed that WAP plays important roles in regulating the proliferation of mammary epithelial cells. The function of WAP has led to speculation that its synthesis and secretion are widespread in a range of species. However, in some species including humans [18], WAP is not synthesized in the mammary gland. It would be interesting to investigate the biological meaning of the absence of WAP synthesis (loss of WAP gene function) in the mammary gland of such species from the standpoint of the molecular evolution of the WAP gene. It is unknown whether or not WAP is synthesized in carnivore species. In the present study, we searched the National Center for Biotechnology Information (NCBI) database for the dog WAP gene and attempted to biochemically identify WAP in dog milk.First, we searched the Canis familiaris-WGS trace archive database with the Discontiguous MegaBLAST program using the pig WAP DNA sequence as a query and obtained 24 hits. The dog WAP gene sequence was predicted by assembling the matched sequence. Then, -Note-

Abstract. Although whey acidic protein (WAP) has been identified in the milk of a range of species, it has been predicted that WAP is not secreted into human milk as a result of critical point mutations within the coding region. In the present study, we first investigated computationally the promoter region of mutated human WAP genes by comparing with those of other known WAP genes. Computational database analyses showed that the human WAP promoter region was highly conserved, as in other species with milk WAP. Next, we evaluated the activity of the human WAP promoter (2.6 kb) using a reporter gene assay. MCF-7 cells were stably transfected with the hWAP/ hGH (human growth hormone) fusion gene, cultured on Matrigel, and treated with lactogenic hormones. Radioimmunoassay detected hGH in the culture medium, indicating that the human WAP promoter was responsible for the lactogenic hormones. The human WAP promoter was significantly more active in MCF-7 cells than the mouse WAP promoter (2.4 kb). The present results provide us with important information on the molecular evolution of milk protein genes.