Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “peanut”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 793 records · Page 44Linked to original sources
PubMed1998

[Storage and use of antioxidants in cereal and peanut bars].

The use of fatty materials in cereal bars gives to them a good energetic value; however they are exposed to oxidative rancidity which can affect their acceptability and nutritional value. So, the purpose of this research was to determine the stability in storage and the effect of antioxidants on three tipes of cereal bars with peanuts. Cereal bars with 18% of peanuts were prepared, with and without antioxidants (BHA + BHT; 100 ppm). Bars were packed in polyprolpilene-aluminium-polythilene bags, and were stored at room temperature (18-20 degrees C) for 90 days. Each 30 days, analysis of water activity (Aw); moisture content, peroxides index, sensory quality (flavor, aroma and appearance) and acceptability, were carried out. Moisture content was similar in all bars (7.6-9.6%) and Aw was higher in the bar which contained expanded amaranthus and antioxidant. At the 60th day of storage, the peroxide values were lower in the bars with antioxidants; only the bar which included expanded amaranthus showed significant differences (16.4 meq/kg in the bar with antioxidant and 25.7 meq/kg for the control bar). The sensory parameters were kept within normal status without differences between the bars with antioxidants and the control ones, along all the storage period. Shelf life of bars CM1 and CM2 was at least of 60 days when they are kept at 18-20 degrees C.

Aluminum↗
PubMed1997

Detection of colorectal neoplasia with peanut-agglutinin (PNA)-reactive carbohydrate structures in rectal mucus.

In contrast to normal colorectal mucosa, peanut-agglutinin-(PNA)-reactive glycoconjugates are commonly expressed in most colorectal carcinomas and in some pre-malignant conditions such as adenomas and ulcerative colitis. Since enzymatically detectable galactose-beta1-3-N-acetyl-galactosamine residues are found in rectal mucus obtained from patients with carcinoma of the large bowel, it was investigated here whether PNA-reactive carbohydrate structures in rectal mucus can be exploited in the detection of colorectal neoplasia. Samples of rectal mucus obtained from 261 randomly selected patients with colorectal symptoms were applied on nitrocellulose filters. The presence of PNA-reactive glycoconjugates in mucus samples was determined by a peroxidase-conjugated PNA-overlay procedure. The results were correlated to findings from total colonoscopy/surgery and histopathology. PNA-reactive carbohydrate structures were detected in 76% of patients with carcinoma (p < 0.005), in 62% of patients with adenoma (p < 0.005), in 69% of patients with inflammatory bowel disease (p < 0.005), and in 38% of patients with hyperplastic polyps (NS), in contrast to 21% of the control subjects with macroscopically normal colorectal mucosa. These results show that PNA-reactive carbohydrate alterations in rectal mucus correlates with neoplastic and hyperproliferative conditions of the colorectal mucosa. The specificity of the PNA test for colorectal neoplasia was 76%. Therefore the use of more discriminate carbohydrate probes are needed for the pre-symptomatic detection of colorectal neoplasia.

Adenoma↗
PubMed1986

Peanut agglutinin. A useful marker for histiocytosis X and interdigitating reticulum cells.

We studied the peanut agglutinin (PNA) staining patterns of histiocytosis X (H-X) (three cases, including one case of Letterer-Siwe disease) and well-characterized cases of malignant histiocytosis (two cases) and monoblastic leukemia (one case) in paraffin-embedded specimens. H-X cells showed staining identical to that of interdigitating reticulum cells, with unique paranuclear and cell surface deposits of reaction products. Thus, H-X cells were easily distinguished from benign macrophage-histiocytes, which show diffuse cytoplasmic staining, and malignant cells of malignant histiocytosis and monoblastic leukemia, which did not stain with PNA, PNA staining proved more useful than Leu-M1 antibody for this purpose, since neither interdigitating reticulum cells in ten reactive lymph nodes nor Langerhans'-type cells in three cases of H-X were stained with Leu-M1 antibody. These observations support a close relationship between H-X cells and interdigitating reticulum cells, and demonstrate the usefulness of PNA for the identification of these cells in paraffin-embedded material.

Adult↗
PubMed1986

Peanut lectin binding in breast carcinoma. Lack of correlation with estrogen receptor content.

Previous reports have shown binding of peanut agglutinin (PNA) by immunoperoxidase techniques in normal, benign proliferative, and malignant breast epithelia. Correlation of binding with maturity, secretory activity, hormonal milieu, and tissue hormone receptor content has been described. To investigate the relationship between PNA staining by the avidin-biotin complex technique and estrogen receptor (ER) content, 79 breast tumors of different types and known tissue ER content were studied. Thirty-eight of 50 ER-positive cases were PNA-positive. Twenty of 29 ER-negative cases were PNA-positive. Statistical analysis shows the two factors to be independent (0.5 less than P less than 0.9). The literature on blood group antigens in breast carcinoma and histochemical applications of PNA is reviewed.

Arachis↗
PubMed1989

Binding of wheat and peanut lectins to human transitional cell carcinomas. Correlation with histopathologic grade, invasion, and DNA ploidy.

The binding of peanut (PNA) and wheat germ (WGA) lectins to tissue sections was examined in biopsy specimens from normal urothelium (ten patients) and from tumor tissue of noninvasive (17 patients) and invasive bladder (31 patients) carcinomas. The results were correlated to DNA content, histopathologic grade, and the presence or absence of invasion. Significant alterations in lectin binding associated with the development of cancer were found. A gradual loss of both PNA and WGA binding was found to correlate with higher grades of atypia (P less than 0.001). The loss of WGA binding was significantly correlated with both tumor aneuploidy (P less than 0.001) and the presence of invasion (P less than 0.05), whereas no significant correlation was found between loss of PNA binding and these variables. We concluded that the loss of WGA binding structures associated with bladder cancer shows a better correlation with known risk factors (aneuploidy and invasion) than the loss of PNA binding does.

Arachis↗
PubMed1992

A new enzyme-linked lectin/mucin antibody sandwich assay (CAM 17.1/WGA) assessed in combination with CA 19-9 and peanut lectin binding assay for the diagnosis of pancreatic cancer.

BACKGROUND: Mucus glycoproteins are often present in the sera of patients with pancreatic cancer, and their detection and quantification can be used in serologic diagnosis. METHODS: A novel enzyme-linked "sandwich" assay (CAM 17.1/WGA) has been developed in which a lectin, wheat germ agglutinin (WGA), is bound to the solid phase to capture serum glycoproteins, and after addition of test sera, a monoclonal antimucin antibody (CAM 17.1) and peroxidase-tagged second antibody are used as a detection system. RESULTS: The test has been applied to sera from 79 patients with pancreatic cancer and 120 controls. The CAM 17.1/WGA assay alone had a sensitivity of 78% and specificity of 76% in the diagnosis of pancreatic cancer. Combination of the CAM 17.1/WGA test with a previously described peanut lectin binding assay (PNA/ELLA) provided a sensitivity of 92% and specificity of 70%, whereas combination of the CAM 17.1/WGA assay with the CA 19-9 radioimmunoassay had a sensitivity of 85% and specificity of 76%. Combination of all three tests had a sensitivity of 94% and specificity of 66%. In nonjaundiced patients, the combination of CAM 17.1/WGA and PNA/ELLA had a sensitivity of 93% and specificity of 79% in the diagnosis of pancreatic cancer. CONCLUSIONS: This new test adds significantly to the armamentarium of serologic tests for pancreatic cancer. These tests are particularly effective when used in combination to detect different mucin-borne carbohydrate antigens. They deserve more widespread use, particularly in examining nonjaundiced patients with unexplained abdominal pain or weight loss.

Adolescent↗
PubMed2002

Natural deuterium distribution in fatty acids isolated from peanut seed oil: a site-specific study by quantitative 2H NMR spectroscopy.

Quantitative (2)H NMR spectroscopy has been used to measure the distribution of deuterium at natural abundance in long-chain fatty acids extracted from the same vegetable oil. Peanut seed oil was selected, due to its suitable oleic and linoleic acid content. The methyl esters of the fatty acids were prepared by transesterification and isolated by modified argentation column chromatography on silica. In order to measure the natural isotopic fractionation of deuterium (D) at the maximum number of positions, the purified methyl oleate and methyl linoleate were chemically cleaved and the (D/H)(i) values determined by quantitative (2)H NMR spectroscopy. It was thus possible to demonstrate that fractionation in deuterium occurs during the desaturation of oleate to linoleate. Furthermore, the previously observed distribution of deuterium at the sites of desaturation is confirmed, as is the alternating pattern of (D/H)(i), which relates to the origin of the pertinent hydrogen atoms. The data obtained are discussed in terms of the kinetic isotopic effects intrinsic to the enzymes-synthetases and desaturases-involved in the biosynthesis of fatty acids.

Chromatography↗
PubMed1986

Biochemical characterization of the major peanut-agglutinin-binding glycoproteins in vertebrate retinae.

Peanut agglutinin (PNA), a lectin that binds D-galactose-beta (1----3) N-acetyl-D-galactosamine disaccharide linkages, selectively labels cone photoreceptors in the retinae of a variety of species. PNA binds consistently to domains of the interphotoreceptor matrix associated with cone, but not rod, inner and outer segments, to cone cell body and axonal membranes, to cone synaptic pedicles, and to portions of the inner plexiform layer. In order to begin the characterization of the molecular species responsible for cone-specific PNA binding, chick, turkey, rat, dog, pig, monkey, and human retinal extracts were separated by SDS-polyacrylamide gel electrophoresis and probed with peroxidase-conjugated PNA. The results reveal the presence of six major groups of PNA-binding glycoproteins ranging from 30 to 88 kilodaltons. Most of these are shared by the seven species examined; however, some interspecies variation is present. Three groups, designated GP39/40, GP42/45, and GP60, are the most intensely labeled by PNA and are common to all species analyzed, while groups GP29/31 and GP88 are less intensely labeled and are present in most but not all of the species investigated. Labeling of the GP54 group is variable but is most consistently associated with extracts of rat and pig retinae. Trypsin treatment, which results in the loss of cone-associated PNA binding in the interphotoreceptor matrix, causes a visually detectable reduction in three of the six groups of PNA-binding glycoproteins in porcine retinal extracts. Of these, GP54 is the most sensitive, being undetectable on PNA-stained blots after only 5 minutes of enzyme exposure; GP88 and GP45 are less sensitive but both are markedly reduced after 15 minutes of trypsinization. Trypsin-sensitive molecules thus may be involved in the establishment of the cone-specific domains of interphotoreceptor matrix identified by PNA binding. These, as well as the other groups of PNA-binding molecules, are being utilized to develop more specific immunologic probes with which to further study of their distribution and function.

Animals↗
PubMed1994

Differential glycosylation of auditory and vestibular hair bundle proteins revealed by peanut agglutinin.

Up to four morphologically distinct types of cross-link are found between the stereocilia in the hair bundles of avian hair cells. These links are involved in mechanotransduction, force transmission across the bundle, and maintenance of hair bundle structure. They appear to be specialisations of the cell coat, but very little is known about their molecular composition. Chick inner ear tissues were therefore screened with a number of different lectins to find markers for specialisations of the hair bundle surface. One lectin, peanut agglutinin (PNA), which recognises the dissacharide Gal beta 1-3GalNAc, was found to be a fairly selective marker for vestibular hair bundles, but it does not stain the stereocilia of auditory hair cells. The staining patterns observed with PNA in the vestibular system closely resemble those seen with a monoclonal antibody (mab) directed against a 275 kD component of the hair cell's apical surface known as the hair-cell antigen (HCA). However, unlike PNA, the mab recognises both vestibular and auditory hair cells. A detailed comparison of the fluorescence staining patterns observed with PNA and the anti-HCA mab indicates that binding sites for both ligands spatially codistribute on the surface of vestibular hair cells. The lectin and the anti-HCA mab binding sites are both sensitive to trypsin treatment, and, with sections of the vestibular system, PNA pretreatment blocks subsequent anti-HCA mab staining. Immunoelectron microscopy of vestibular hair bundles shows that PNA and the anti-HCA mab both label a type of cross-link known as the shaft connector. This link type is present on both auditory and vestibular hair bundles but reacts with PNA only in the vestibular system. The lectin jacalin, which has greater specificity for Gal beta 1-3GalNAc than does PNA, also only labels vestibular and not auditory hair bundles. Although terminal sialic acid residues can block both PNA and jacalin binding, neuraminidase treatment does not unmask cryptic binding sites for these lectins on auditory hair cells but does reveal PNA and jacalin staining at a number of other locations in the inner ear. The results obtained with the lectins PNA and jacalin indicate that either the HCA or other components of the shaft links are differentially glycosylated in the vestibular and auditory epithelia of the bird. The functional significance for such a difference in glycosylation remains to be determined, but auditory and vestibular hair cells operate over different frequency ranges, and variations in glycosylation might confer different micromechanical properties on the hair bundles in these two systems.

Animals↗
PubMed1982

Functional and phenotypic properties of subpopulations of murine thymocytes. I. The bulk of peanut agglutinin-positive Lyt-1,2,3 thymocytes lacks precursors of cytotoxic T lymphocytes responsive to interleukin 2 (T cell growth factor).

Thymocytes were separate according to their surface phenotype and tested for cytotoxic T lymphocyte (CTL) precursor function by stimulation with allogeneic or hapten-coupled cells, with or without addition of T cell growth factor (interleukin 2). The data show that only a minor subpopulation of thymocytes agglutinated by peanut agglutinin, expressing relatively high amounts of H-2K antigen, contained CTL precursors. The remaining population, approximately 80%, could not be induced to generate CTL, even in the presence of interleukin 2.

Animals↗
PubMed1983

T lymphocyte lines producing or vaccinating against autoimmune encephalomyelitis (EAE). Functional activation induces peanut agglutinin receptors and accumulation in the brain and thymus of line cells.

We studied lines of rat T cells, specifically reactive against myelin basic protein (BP), that were functional in mediating autoimmune encephalomyelitis or in vaccinating rats against induction of active EAE. Herein we report that these functions depended on activation of the cells by incubation with BP or with a T cell mitogen prior to inoculation into recipient rats. Activation was accompanied by the exposure of membrane-binding sites specific for the lectin peanut agglutinin. Accumulation of activated line cells in the central nervous system and thymus gland was observed.

Animals↗
PubMed1983

Relationship between mouse lymphocyte receptors for peanut agglutinin (PNA) and Helix pomatia agglutinin (HPA).

The relationship between mouse lymphocyte receptors for peanut agglutinin (PNA) and Helix pomatia agglutinin (HPA) has been investigated by immunofluorescence (cocapping) and radiolabeling. In neuraminidase-treated and untreated thymocytes there are two groups of glycoproteins which bind roughly equivalent amounts of PNA. One group also carries all the detectable receptors for HPA, the other binds only PNA. Binding inhibition experiments suggest that PNA and HPA receptors are in close proximity on the shared glycoproteins. The same two groups of receptors are present on 35-40% of neuraminidase-treated spleen lymphoid cells, mainly immunoglobulin (Ig)-negative lymphocytes. Almost all B cells have only PNA-specific receptors. Five-12% of the untreated spleen cells appreciably bind PNA and only a few bind HPA. Solubilized glycoproteins specific for PNA or HPA were compared by sodium dodecyl sulfate polyacrylamide gel electrophoresis and autoradiography. The major PNA-specific radioiodinated glycoproteins of neuraminidase-treated thymocytes, as isolated by affinity chromatography, consist of the 185-kDa and 195-kDa components of the T200 antigen and of two (diffuse) components of about 140 and 120-125 kDa. All these molecules also bind to HPA-Sepharose, with the exception of the 185 kDa component, which is probably the main constituent of the "pure" PNA receptors on the intact thymocytes. In gels directly labeled with radioactive lectins, the only band strongly labeled by PNA and HPA is the diffuse 140-kDa band. The band at 120 kDa is well labeled by PNA, but all the other components are weakly labeled. The mobility of the 140- and 120-kDa bands depends strongly on neuraminidase-treatment. These bands cannot be detected in gels of untreated thymocytes, but a major HPA-and PNA-specific band of lower molecular weight can be labeled after treating the gels with neuraminidase. The factors determining the differences in labeling pattern obtained by different methods as well as the nature of PNA and HPA binding sites are discussed. The same major PNA- and HPA-binding glycoproteins (apart from minor differences) are present on neuraminidase-treated Ig-negative spleen lymphocytes. The major PNA-binding protein of B lymphocytes appears to correspond to the 225-kDa ("B220") antigen specific for these cells.

Animals↗
PubMed1984

Surface carbohydrate epitopes of Thy-1.1 and Thy-1.2 thymocytes are distinguished by a monoclonal antibody with a specificity common to peanut agglutinin.

NIMF4-31.7 is a monoclonal IgM antibody with affinity for terminal galactose residues of membrane glycoproteins, Sepharose and agarose. It is cytotoxic for a subpopulation of murine thymocytes and peripheral lymphocytes, corresponding to the peanut agglutinin-positive population, but reacts with a majority of cells after neuraminidase treatment. It has revealed a genetic linkage between the Thy-1 locus and quantitative expression of carbohydrate determinants on the thymocyte membrane.

Animals↗
PubMed1985

Effect of thymulin on intracellular cyclic nucleotides and prostaglandins E2 in peanut agglutinin-fractionated thymocytes.

Prostaglandin E2 (PGE2) and other selected agents which elevate intracellular cyclic AMP (cAMP) levels have been demonstrated to induce the appearance of surface markers in immature T lymphocytes. Thymic hormones, which are the natural inducers of these markers, have long been hypothesized to act through the increase of cAMP levels. We have approached this area of investigation by studying the effects of thymulin (a serum thymus-derived factor, coupled with Zinc) on intracellular cAMP and cyclic GMP (cGMP) levels (expressed as cAMP/cGMP ratio) and on the release of PGE2 in different thymocyte subpopulations. Thymocytes were fractionated by the peanut agglutinin (PNA) technique into cortical immature PNA+ and medullary mature PNA- thymocytes. The data presented in this report show that thymulin is able to increase the cAMP/cGMP ratio in PNA+ and in unfractionated thymocytes, depending on its concentration, but not in PNA- thymic cells. Conversely, it is able to increase the release of PGE2 by PNA- thymocytes but not by PNA+ and unfractionated thymic lymphocytes. These results are consistent with the hypothesis that thymulin could act through different mechanisms depending on the differentiation stage of its target cells. In fact, it could be suggested that immature T cells could be activated by thymulin thereby increasing the cAMP/cGMP ratio, whereas more mature T cells would be further differentiated by thymulin through enhanced release of PGE2.

Animals↗
PubMed1990

Purification and characterization of a peanut-agglutinin-binding pancreatic-cancer-related serum mucus glycoprotein.

A high-molecular-weight (approximately 3.5 x 10(3) kDa) peanut agglutinin (PNA)-binding glycoprotein was previously identified as a tumour marker in pancreatic cancer sera. In the present study the density of this glycoprotein has been estimated and further analysis performed using sequential lectin blotting combined with serial mild acid hydrolysis followed by repeated Smith degradation. This has allowed partial in-situ characterization of the carbohydrate side-chains. The PNA-binding glycoprotein variably expresses the blood group H and sialylated Lewis a antigens. H and sialyl Lea expression disappeared after mild acid hydrolysis and T (PNA acceptor) disappeared after the first Smith degradation step. T (beta gal(1-3)alpha galNAc) expression reappeared after a second Smith degradation, suggesting that the backbone regions of the mucin side-chains with this core sequence are built up by the further addition of at least 2 monosaccharides. A model has been constructed showing the minimum variations in side chain structure that would explain the results of the serial degradation and lectin blotting. Purification and caesium chloride density gradient centrifugation show that the intact PNA-binding glycoprotein has a density of greater than 1.48 g/ml, characteristic of a mucin. The development of assays using a panel of monoclonal antibodies (MAbs) or lectins directed against the different carbohydrate epitopes expressed on this mucin may provide better diagnostic accuracy for pancreatic cancer than current marker assays which rely on detection of a single epitope.

Antigens, Tumor-Associated, Carbohydrate↗
PubMed1982

Isolation and characterization of peanut agglutinin-resistant embryonal carcinoma cell-surface variants.

The isolation and characterization of variant embryonal carcinoma (EC) cells possessing altered cell-surface structures is described. The lectin peanut agglutinin (PNA), which binds to EC cells but not their differentiated derivatives, was used to select the variants. Clones resistant to the cytotoxic effect of PNA were isolated at a frequency of 4 X 10(-5) following mutagenesis. The resistant phenotype was stable in the absence of selection in all eight clones tested. The increased frequency of resistant clones following mutagenesis and the stability of the phenotype suggests a mutational origin. Somatic cell hybrids constructed between wild-type cells and two different PNA-resistant cell lines were sensitive to PNA; this suggests that the resistant phenotype is recessive. Binding assays demonstrated that resistant cells exhibited a twofold to fourfold reduction in the total amount of PNA bound. Together with the recessive behavior of the phenotype, this suggests that resistant cells are deficient for PNA receptors. The PNA-resistant cells also showed reduced binding of monoclonal antibody against stage-specific embryonic antigen 1 (SSEA-1) in indirect cytotoxicity tests. All eight PNA-resistant lines isolated were tumorigenic in syngeneic mice and gave rise to well-differentiated teratocarcinomas. The PNA-resistant cells behaved like their wild-type parents in a cell recognition assay; when incubated in suspension with endodermal cells, they sorted out to form simple embryoid bodies (a core of EC cells surrounded by an endodermal rind). Thus, EC cells can form tumors, differentiate, and recognize differentiated cells in a sorting assay despite a reduction in expression of the embryo-specific cell surface structures (s) that bind PNA and anti-SSEA-1 antibody.

Animals↗
PubMed1992

Use of peanut lectin and rat mammary stem cell lines to identify a cellular differentiation pathway for the alveolar cell in the rat mammary gland.

The presence of the carbohydrate receptor for PNL has been used to identify the previously described morphological types of epithelial cell produced as the stem cell line rat mammary 25 (Rama 25) differentiates to casein secretory alveolar-like cells in vitro. Thus when cultures of the epithelial stem cell line Rama 25 are treated with neuraminidase, fluorescently-conjugated PNL fails to stain cuboidal cells, stains weakly grey cells, and stains strongly the surface of dark cells. When superconfluent cultures of Rama 25 are treated with dimethyl sulfoxide or retinoic acid and prolactin, estradiol, hydrocortisone, and insulin to induce differentiation to alveolar cells, PNL stains strongly the untreated surfaces of droplet cells and casein-secreting vacuolated cells. PNL-staining of the derivative cell lines with truncated cellular pathways, and quantitative binding of [125I]-labeled PNL to the cultured cells are consistent with this cellular staining pattern. The presence of the carbohydrate receptor for peanut lectin (PNL) has also been used to identify specific epithelial cell types in different mammary structures of the developing rat mammary gland, as they differentiate to casein secretory alveolar cells in vivo. Thus when different structures of the developing rat mammary gland are treated with neuraminidase, peroxidase-conjugated PNL fails to stain histochemically the majority of epithelial cells in ducts, stains the cytoplasm of the majority of epithelial cells in terminal end-buds (TEBs), and stains strongly the luminal surfaces of the majority of epithelial cells in alveolar buds (ABs). PNL also stains the untreated luminal surfaces of alveolar cells, whether or not the cells can be stained with a monoclonal antibody to rat beta-casein. Stimulation of mammary differentiation by an analogue of ethyl retinoate or by perphenazine causes cells in end-buds to bind PNL without the necessity for their desialylation similar to that seen in casein secretory alveoli of lactating rats. In conclusion the different interconverting cell types of Rama 25 which form a pathway to casein-secretory cells in vitro are thus equated with recognisable epithelial cell types in vivo. These results suggest that casein-secretory cells in vivo are generated by similar successive interconversions between the major epithelial cell types present in the different mammary structures in the order: ducts, TEBs, ABs, alveoli, and secretory alveoli.

Animals↗
PubMed1987

Role of peanut-lectin-affinity molecules (PLAM) on primordial germ cells in the initial determination of sex in anura.

Peanut lectin (PNA) or N-acetylgalactosamine (galNA, a part of the disaccharide unit which is recognized by PNA) was injected into the coelomic cavity of anuran larvae at the developmental stages during which the genital ridges were growing, and the effect of these compounds on the initial determination of gonadal sex was examined. The treatment with PNA tended to inhibit (or perturb) the expression of feminizing gene(s) in Rana japonica, and of both feminizing and masculinizing genes in R. nigromaculata. In contrast, treatment with galNA suppressed the expression of masculinizing gene(s) considerably. In terms of the initial determination of gonadal sex during normal development, these results suggest that the PNA-affinity molecule (PLAM) of primordial germ cells acts as a trigger for the expression of genes that control sexual differentiation of somatic cells. Furthermore, the somatic cells (perhaps mesenchymal and/or epithelial cells), which respond to the stimulus via the PLAM of primordial germ cells, may differ in terms of the threshold for such a response between genetic males and females. This result suggests the mesenchymal and/or epithelial cells are not sexually predetermined, but rather that sexual determination follows the response to some signal(s) mediated by the PLAM.

Acetylgalactosamine↗