Microheterogeneity of Human Alphafetoprotein

Bręborowicz, J

doi:10.1159/000217540

Cited by 36 publications

(11 citation statements)

References 21 publications

(36 reference statements)

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“…There are many subtypes of AFP; lectin-reactive AFP (eg, AFP-L3) is AFP bound to a sugar group that binds a specific lectin 42. Lectins are proteins with a particular affinity for specific sugar moieties 43.…”

Section: Other Germ Cell Tumor Markersmentioning

confidence: 99%

Role of biochemical markers in testicular cancer: diagnosis, staging, and surveillance

Milose¹,

Filson²,

Weizer³

et al. 2011

OAJU

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Testis cancer is one of the few solid organ malignancies for which reliable serum tumor markers are available to help guide disease management. Human chorionic gonadotropin, alpha fetoprotein, and lactate dehydrogenase play crucial roles in diagnosis, staging, prognosis, monitoring treatment response, and surveillance of seminomatous and nonseminomatous germ cell tumors. Herein we discuss the clinical applications of germ cell tumor markers, the limitations of these markers in the management of this disease, and additional serum molecules that have been identified with potential roles as novel germ cell tumor markers.

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Section: Other Germ Cell Tumor Markersmentioning

confidence: 99%

Role of biochemical markers in testicular cancer: diagnosis, staging, and surveillance

Milose¹,

Filson²,

Weizer³

et al. 2011

OAJU

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“…Initially, some of the different forms have been attributed to carbohydrate microheterogeneity and variations in isoelectric points (Smith and Kelleher, 1980;Crandall, 1981). Some AFP isoforms were lectin glycoforms that were detected and isolated by isoelectric focusing, electrophoresis, and chromate-graphic methods (Breborowicz, 1988;Taketa et al, 1998). Other isoforms were detected following high-pressure liquid chromatography (HPLC), and lectin, heavy metal, and hydrophobic solid phase separation methods.…”

Section: Structural Variantsmentioning

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 is a very large protein and has several surface epitopes 7. The different molecular forms of (alpha) fetoprotein in benign liver disease, hepatoma, germ cell tumours, and hepatic metastases from colorectal neoplasms can be differentiated by their lectin binding properties8 or by monoclonal antibodies, which might offer a better prospect of establishing the source of a raised serum (alpha) fetoprotein concentration 10…”

Section: Discussionmentioning

confidence: 99%

Lesson of the Week: Failure of normalisation of (alpha) fetoprotein concentration after successful treatment of teratoma

Pandha

Wasan²,

Harrington³

et al. 1995

BMJ

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Microheterogeneity of Human Alphafetoprotein

Cited by 36 publications

References 21 publications

Role of biochemical markers in testicular cancer: diagnosis, staging, and surveillance

Role of biochemical markers in testicular cancer: diagnosis, staging, and surveillance

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

Lesson of the Week: Failure of normalisation of (alpha) fetoprotein concentration after successful treatment of teratoma

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