Alpha-fetoprotein can regulate growth in the uterus of the immature and adult ovariectomized mouse

Mizejewski, Gerald J.; Warner, Abby

doi:10.1530/jrf.0.0850177

Cited by 27 publications

(7 citation statements)

References 15 publications

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“…AFP, a tumor‐associated fetal protein is known to be associated with the successful completion of term pregnancies in mammals and even minute amounts of AFP may still be necessary during human pregnancy (Sher & Shohat 1997). AFP serves as a dual regulator of growth, capable of both enhancement and inhibition (Mizejewski & Warner 1988). The capability of both up and down modulation of growth and differentiation as a dose‐dependent function of AFP has been demonstrated in a multitude of cell types including placental, ovarian, uterine, lymphoid, epidermal, endothelial, testicular, breast, and liver (Keel et al .…”

Section: Discussionmentioning

confidence: 99%

Alpha‐fetoprotein is dynamically expressed in rat pancreas during development

Liu

Guo

et al. 2007

Dev Growth Differ

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To identify proteins involved in pancreatic development, we used a differential proteomics approach by comparing pancreatic extracts from four biologically significant stages of development: embryonic day (E) 15.5, E18.5, postnatal (P) days 0 and adult. By two-dimensional gel electrophoresis (2D-E) and MALDI-TOF MS (Matrix Assisted Laser Desorption/Ionization Time-Of-Flight Mass Spectrometry) following database searching and protein annotation, 15 proteins were identified as being differently expressed in the pancreas between the four phases. The expression pattern and the localization of alpha-fetoprotein (AFP), one of significant changed proteins observed, were further determined. Four isoforms of AFP (72 kDa, 60 kDa, 48 kDa and 37 kDa) were found by Western blotting in the pancreas tested, most of them showed a stronger signal in E18.5 followed by a steady decrease and only a 60-kDa isoform was detected in the adult pancreas. Immunolocalization for AFP revealed that a positive reactivity was detectable at E15.5 pancreas, became stronger in the cytoplasm of mesenchyme cells at E18.5, and declined after birth to a nearly undetectable level in adults. The dynamic expression of AFP in rat pancreas from different stages indicates that AFP might be involved in some aspects of pancreatic development.

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Section: Discussionmentioning

confidence: 99%

Alpha‐fetoprotein is dynamically expressed in rat pancreas during development

Liu

Guo

et al. 2007

Dev Growth Differ

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“…The physiological role of AFP is not defini tively established but recent data show that AFP can regulate growth in a variety of tis sues, including cells of the immune system [27] , and can act alone or synergistically with other growth factors [28,29], In addition, we have previously demonstrated that AFP, through its interaction with specific cell recep tors, regulates and enhances the entry of fatty acids into normal and malignant growing cells [30][31][32]. This function may be critical during early embryonic growth, at a time when AFP is the major fatty acid carrier protein avail able, the tissue requirements for polyunsatu rated fatty acids, as in differentiating muscle cells, is very high and the metabolic pathways of fatty acid synthesis, proper to adult tissues, have not yet become operational.…”

Section: Discussionmentioning

confidence: 99%

Alpha-Fetoprotein Binding and Uptake by Primary Cultures of Human Skeletal Muscle

Lorenzo¹,

Geuskens²,

Macho³

et al. 1996

Tumor Biol

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Α-Fetoprotein (AFP), a serum Α-globulin mainly synthesized by the fetal liver and the yolk sac, is the major carrier of poly-unsaturated fatty acids during embryo-fetal development. One property characteristic of fetal cells undergoing growth and differentiation is their ability to bind and internalize AFP. In the present work, we have studied the binding and endocy-tosis of AFP by human muscular cells developing in vitro. Primary cultures of human skeletal muscle, obtained from biopsies and examined at two stages of differentiation (myoblasts and myotubes), were incubated for different times, at 0 and 37 ° C, with a colloidal-gold-conjugated human AFP probe and studied by light and electron microscopy, as well as by laser scanning confocal microscopy in the reflection mode. The results obtained show that (a) human myoblasts in primary culture bind and internalize the protein, probably through specific AFP receptors, (b) this property is strongly reduced or lost in well-differentiated myotubes, and (c) AFP is also bound, throughout culture development, to the extracellular matrix of fusing myoblasts and differentiated myotubes. The physiological significance of AFP uptake by human myoblasts undergoing growth and differentiation may be based on the ability of AFP to carry and deliver fatty acids to fetal cells.

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“…The authors concluded that AFP was a specific inhibitor of the multiplication of cells that were E2 sensitive for growth. Because of such reports, the author of this atlas chapter undertook a series of studies to investigate and hopefully elucidate the E2-sensitive growth inhibitory properties of AFP in vivo (Mizejewski et al, 1983(Mizejewski et al, , 1986Mizejewski and Warner, 1989;Jacobson et al, 1990a;Mizejewski et al, 1990;Allen et al, 1993). These studies concluded that rodent and human AFP contained an encrypted (occult) E2-sensitive growth regulatory site that is induced to emerge following exposure to high estrogen concentrations Mizejewski et al, 1996;Vakharia and Mizejewski, 2000).…”

Section: G) Afp Peptide Sites For Hormones and Growth Factor Bindingmentioning

confidence: 99%

Mapping of Structure-Function Peptide Sites on the Human Alpha-fetoprotein Amino Acid Sequence

Mizejewski¹

2011

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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The structure of alpha-fetoprotein (AFP) is presen-ted in light of AFP membership and position in the albuminoid gene family in comparison to other gene family members. Ontogenetic AFP gene expression is reviewed considering AFP mRNA presence in various tissues at different times during development. The multiple molecular variant forms of AFP are discussed in relation to published reports of AFP binding proteins and cell surface receptors. The atlas further shows AFP as a protein consisting of multiple peptide-cassettes consisting of amino acid (AA) sequence stretches matched to peptide segments on prohormones and biological response modifier proteins. Such AFP peptide segments could potentially serve as delivery agents which could target vascular, neuroendocrine, or gastrointestinal cells. A discussion follows in which peptide epitopes, extracellular matrix proteins, serine proteases, extracellular matrix, and cellular adhesion AA identity sites on AFP are considered. The AFP molecule is also viewed as a carrier/ transport protein based on AA sequence comparison of various proteins that bind hydropho-bic ligands and heavy metals similar to AFP binding of such components. An analysis of trans-cription factors, tumor suppressors, and AA-rich motifs follows, interfaced with dimerization and nuclear localization sequence matches identified on the AFP molecule. Emphasis is further placed upon homeodomain and apoptosis AA sequence identi-ties given that AFP serves as a fetal, phasespecific protein throughout embryogenesis, histogenesis, and organogenesis. AFP AA sequences are further presented as peptide identification sites for Mapping of Structure-Function Peptide Sites on the Human Alpha-fetoprotein Amino Acid SequenceMizejewski GJ Atlas Genet Cytogenet Oncol Haematol. 2010; 14(2) 170 growth factors, receptors, cytoskeletal proteins, and chemo-kines. A closing discussion summarizes the multi-ple and varied motifs of peptide sequences matched to AAs on each of AFP's three domains. This study indicates that short peptide segments, in addition to full-length AFP, and domain and subdomain fragments of AFP, could be employed as functional agents to help unravel the complexity of biological roles ascribed to human AFP.

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Alpha-fetoprotein can regulate growth in the uterus of the immature and adult ovariectomized mouse

Cited by 27 publications

References 15 publications

Alpha‐fetoprotein is dynamically expressed in rat pancreas during development

Alpha‐fetoprotein is dynamically expressed in rat pancreas during development

Alpha-Fetoprotein Binding and Uptake by Primary Cultures of Human Skeletal Muscle

Mapping of Structure-Function Peptide Sites on the Human Alpha-fetoprotein Amino Acid Sequence

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