You will see from earlier posts that the issue is a research article that was published in 2005 that found that there is 1-2% difference in DNA sequence between humans and chimps and yet 80% of the proteins are different. From the limited number of comparisons that were made at that time it emerged that for most of these proteins the differences were very small say 2% between human and chimp proteins. The article states that these differences were too small to account for the difference in phenotype between humans and chimps. The fact that there was such a small difference in DNA sequence and such a small difference in the quality not the quantity of the proteins in the chimp suggested that all is at it should be and Neo-Darwinism could stand. The article suggested that the difference in phenotype (which I put at about 60% at least) must be due to small differences in a few regulatory genes in early development. Indeed they must be small differences because there is only 1-2% difference in DNA sequence overall, and this is already needed to account for the differences in 80% of the proteins.

So I have now identified 10 genes that are expressed in the mammalian placenta and I am going to compare in the gene databases the proteins synthesized from these genes. I suspect however that again I will find that there is about a 1% difference in the DNA sequence and a 2-3% difference in the amino acid sequence of the proteins. My own theory about this is that the fact that there is a small percentage of difference in so many proteins (80%) does indeed account for the fact that there is a 60% (at least) difference in phenotype between human and chimp. Take a simple example: If there is a 2% difference in proteins between 80% of the proteins in two species then that could arguably account for an 80 x 2= 160% difference in phenotype between the two species. This is not strictly a formal mathematical permutation or combination but still as a matter of common sense it could account for the fact that there is a 60% (at least) difference in phenotype between human and chimp. Basically very small differences in a large proportion of all the proteins in an organism are responsible for its phenotype.

Which means that six million years ago in just one generation all these small insignificant mutations must have all occurred simultaneously for the human being to differentiate from the chimpanzee. The image above which presents the standard theory of Neo-Darwinism that the human gradually evolved over six million years and started to stand upright simply doesn't stack up with the fact that the differences in DNA sequence and the great bulk of the proteins in human and chimp are insignificantly small. It doesn't stack up because if these insignificantly small mutations happened randomly in dribs and drabs over millions of years then there could not have been a complete differentiation between the two species. They would have been able to continue to interbreed and the fossil record would show all sorts of intermediate hybrids. The only way to account for the 60% (at least) difference in phenotype between human and chimp is if all the insignificantly small mutations happened at once to create two different creatures. It is submitted that this demonstrates that Neo-Darwinism is clearly wrong, and if you can't accept that then surely you must concede that Neo-Darwinism offers no explanation for the fact that two creatures so similar in their genome and proteins could be two separate species so totally different and distinct in their phenotype.

In fact the orthodox explanation that a small difference in a few developmental genes in embryogenesis are responsible for the differentiation of human and chimp species would be the strongest argument possible for intelligent design, for these same small differences in only one or a few regulatory genes would be responsible for the differentiation of all the mammal species and these could not possibly be random cheemical mutations.




Global gene expression analysis and regulation of the principal genes expressed in bovine placenta in relation to the transcription factor AP-2 family

We detected gestational-stage-specific gene expression profiles in bovine placentomes using a combination of microarray and in silico analysis. In silico analysis indicated that the AP-2 family may be a consensus regulator for the gene cluster that characteristically appears in bovine placenta as gestation progresses. In particular, TFAP2A and TFAP2B may be involved in regulating binucleate cell-specific genes such as CSH1, some PAG or SULT1E1. These results suggest that the AP-2 family is a specific transcription factor for clusters of crucial placental genes. This is the first evidence that TFAP2A may regulate the differentiation and specific functions of BNC in bovine placenta.

A Human Placenta-specific ATP-Binding Cassette Gene (ABCP) on Chromosome 4q22 That Is Involved in Multidrug Resistance

We characterized a new human ATP-binding cassette (ABC) transporter gene that is highly expressed in the placenta. The gene, ABCP, produces two transcripts that differ at the 5′ end and encode the same 655-amino acid protein. The predicted protein is closely related to the Drosophila white and yeast ADP1 genes and is a member of a subfamily that includes several multidrug resistance transporters. ABCPwhite, and ADP1 all have a single ATP-binding domain at the NH2terminus and a single COOH-terminal set of transmembrane segments. ABCP maps to human chromosome 4q22, between the markers D4S2462 and D4S1557, and the murine gene (Abcp) is located on chromosome 6 28–29 cM from the centromere. ABCP defines a new syntenic segment between human chromosome 4 and mouse chromosome 6. The abundant expression of this gene in the placenta suggests that the protein product has an important role in transport of specific molecule(s) into or out of this tissue.

Identification of a novel member of the TGF-beta superfamily highly expressed in human placenta

While conducting a gene discovery effort targeted to transcripts of the prevalent and intermediate frequency classes in placenta throughout gestation, we identified a novel member of the TGF-β superfamily that is expressed at high levels in human placenta. Hence, we named this factor `Placental Transforming Growth Factor Beta' (PTGFB). The full-length sequence of the 1.2-kb PTGFB mRNA has the potential of encoding a putative pre-pro-PTGFB protein of 295 amino acids and a putative mature PTGFB protein of 112 amino acids. Multiple sequence alignments of PTGFB and representative members of all TGF-β subfamilies evidenced a number of conserved residues, including the seven cysteines that are almost invariant in all members of the TGF-β superfamily. The single-copy PTGFB gene was shown to be composed of only two exons of 309 bp and 891 bp, separated by a 2.9-kb intron. The gene was localized to chromosome 19p12-13.1 by fluorescence in-situ hybridization. Northern analyses revealed a complex tissue-specific pattern of expression and a second transcript of 1.9 kb that is predominant in adult skeletal muscle. Most importantly, the 1.2-kb PTGFB transcript was shown to be expressed in placenta at much higher levels than in any other human fetal or adult tissue surveyed.

Expression of P-glycoprotein in Human Placenta: Relation to Genetic Polymorphism of the Multidrug Resistance (MDR)-1 Gene

To evaluate whether mutations in the human multidrug resistance (MDR)-1 gene correlate with placental P-glycoprotein (PGP) expression, we sequenced the MDR-1 cDNA and measured PGP expression by Western blotting in 100 placentas obtained from Japanese women.  When genotype results were compared between Caucasians and Japanese, ethnic differences in the frequency of polymorphism in the MDR-1 gene were suspected.

Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells

The complete 1,210-amino acid sequence of the human epidermal growth factor (EGF) receptor precursor, deduced from cDNA clones derived from placental and A431 carcinoma cells, reveals close similarity between the entire predicted ν-erb-B mRNA oncogene product and the receptor transmembrane and cytoplasmic domains. 

Differential expression of HLA-E, HLA-F, and HLA-G transcripts in human tissue

The data presented here demonstrated that the HLA-G class I gene is unique among the members of the human class I gene family in that its expression is restricted to extraembryonic tissues during gestation. Furthermore, the pattern of HLA-G expression in these tissues changes as gestation proceeds. During first trimester HLA-G is expressed within the placenta and not within the extravillous membrane. At term, the pattern of the HLA-G expression is reversed, extravillous membrane expressed HLA-G while placenta does not. Another non-HLA-A, -B, -C class I gene, HLA-E, is also expressed by extraembryonic tissues. Unlike HLA-G, HLA-E is expressed by both placenta and extravillous membrane at first trimester and at term. These results raise the intriguing possbility that the HLA-G-encoded molecule has a role in embryonic development and/or the fetal-maternal immune response.

Cloning of a New Member of the Insulin Gene Superfamily (INSL4) Expressed in Human Placenta

A new member of the insulin gene superfamily was identified by screening a subtracted cDNA library of first-trimester human placenta and, hence, was tentatively named early placenta insulin-like peptide (EPIL). In this paper, we report the cloning and sequencing of the EPIL cDNA and the EPIL gene (INSL4). Comparison of the deduced amino acid sequence of the early placenta insulin-like peptide revealed significant overall and structural homologies with members of the insulin-like hormone superfamily. Moreover, the organization of the early placenta insulin-like gene, which is composed of two exons and one intron, is similar to that of insulin and relaxin. Byin situhybridization, the INSL4 gene was assigned to band p24 of the short arm of chromosome 9. RT-PCR analysis of EPIL tissue distribution revealed that its transcripts are expressed in the placenta and uterus.

Identification of a novel MHC class I gene, Mamu-AG, expressed in the placenta of a primate with an inactivated G locus.

In this study, we report the identification of a novel nonclassical MHC class I locus expressed in the placenta of the rhesus monkey, Mamu-AG (Macaca mulatta-AG). Although unrelated to HLA-G, Mamu-AG encodes glycoproteins with all of the characteristics of HLA-G. These Mamu-AG glycoproteins are limited in their diversity, possess truncated cytoplasmic domains, are the products of alternatively spliced mRNAs, and their expression is restricted to the placenta. Taken together, these data suggest that convergent evolution may have resulted in the expression of a unique nonclassical MHC class I molecule in the rhesus monkey placenta, and that the common structural features of Mamu-AG and HLA-G may be functionally significant.

Secreted placental alkaline phosphatase: a powerful new quantitative indicator of gene expression in eukaryotic cells

This paper describes a novel eukaryotic reporter gene, secreted alkaline phosphatase (SEAP). In transient expression experiments using transfected mammalian cells, we demonstrate that SEAP yields results that are qualitatively and quantitatively similar, at both the mRNA and protein levels, to parallel results obtained using established reporter genes. 

PPARγ Is Required for Placental, Cardiac, and Adipose Tissue Development

The nuclear hormone receptor PPARγ promotes adipogenesis and macrophage differentiation and is a primary pharmacological target in the treatment of type II diabetes. Here, we show that PPARγ gene knockout results in two independent lethal phases. Initially, PPARγ deficiency interferes with terminal differentiation of the trophoblast and placental vascularization, leading to severe myocardial thinning and death by E10.0. Supplementing PPARγ null embryos with wild-type placentas via aggregation with tetraploid embryos corrects the cardiac defect, implicating a previously unrecognized dependence of the developing heart on a functional placenta.

Human cholesterol side-chain cleavage enzyme, P450scc: cDNA cloning, assignment of the gene to chromosome 15, and expression in the placenta

 P450scc cDNA was used to probe DNA from a panel of mouse-human somatic cell hybrids, showing that the single human P450scc gene lies on chromosome 15. The human P450scc gene is expressed in the placenta in early and midgestation; primary cultures of placental tissue indicate P450scc mRNA accumulates in response to cyclic AMP.







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