Pineda-Salgado L et al. (2005), Expression of Panza, an alpha2-macroglobulin, i...

XB-ART-1128

Gene Expr Patterns 2005 Dec 01;61:3-10. doi: 10.1016/j.modgep.2005.09.001.

Show Gene links Show Anatomy links

Expression of Panza, an alpha2-macroglobulin, in a restricted dorsal domain of the primitive gut in Xenopus laevis.

Pineda-Salgado L , Craig EJ , Blank RB , Kessler DS .

???displayArticle.abstract???
Alpha2-macroglobulin is a major serum protein with diverse functions, including inhibition of protease activity and binding of growth factors, cytokines, and disease factors. We have cloned and characterized Panza, a new Xenopus laevis alpha2-macroglobulin. Panza has 56-60% amino acid similarity with previously identified Xenopus, mouse, rat and human alpha2-macroglobulins, indicating that Panza is a new member of the alpha2-macroglobulin family. Panza mRNA is first detected at the beginning of neurulation in the dorsal endoderm lining the primitive gut (archenteron roof). At the completion of neurulation and continuing through the late tadpole stage, Panza is restricted to a dorsal domain of the gut endoderm adjacent to the notochord and extending along the entire anterior-posterior axis. With outgrowth of the tailbud, Panza expression persists in the chordaneural hinge at the posterior end of the differentiating notochord and extends into the floor plate of the posterior neural tube. As gut coiling commences, Panza expression is initiated in the liver, and the dorsal domain of Panza expression becomes limited to the midgut and hindgut. With further gut coiling, strong Panza expression persists in the liver, but is lost from other regions of the gut. The expression of Panza in endodermal cells adjacent to the notochord points to a potential role for Panza in signal modulation and/or morphogenesis of the primitive gut.

???displayArticle.pubmedLink??? 16275122
???displayArticle.pmcLink??? PMC1351133
???displayArticle.link??? Gene Expr Patterns
???displayArticle.grants??? [+]

Species referenced: Xenopus laevis
Genes referenced: a2m a2ml1

???attribute.lit??? ???displayArticles.show???

	Fig. 2. Embryonic expression of Panza and Edd. Whole-mount in situ hybridization for Panza (A,A1,A2,C,E,E1,E2,G,I) and Edd (B,B1,B2,D,F,F1,F2,H,J) at stages 14 (A,A1,A2,B,B1,B2), 17 (C,D), 20 (E,E1,E2,F,F1,F2), 26 (G,H), and 33 (I,J). Panza expression is first detected at the neurula stage in the dorsal primitive gut (archenteron roof) extending from the oral evagination to the blastopore, with expression extending more laterally in the posterior gut. With elongation of the body axis, Panza extends along the entire anterior–posterior axis in the dorsal gut endoderm, narrower in the anterior gut and gradually broadening in the posterior gut. Panza is also expressed in the chordaneural hinge, extending into the floorplate of the posterior neural tube (arrowheads). Edd is expressed throughout the dorsal, lateral and ventral endoderm, but not in the neural tube. (A–J) Lateral views of cleared embryos with anterior left are shown. (A1–F2) Transverse sections (dorsal up) of stained embryos at the axial levels indicated by dotted lines in (A,B,E,F). fp, Floorplate; n, notochord.
	Fig. 3. Panza expression adjacent to the notochord. (A) Double staining for Panza (blue) by whole-mount in situ hybridization and notochord (brown) by immunohistochemistry using the Tor70 monoclonal antibody. Panza is expressed in the gut endoderm adjacent to the notochord and extends around the posterior tip of the notochord into the floorplate of the posterior neural tube. (A1–A4) Transverse sections of double-stained embryos (stage 33) at the axial levels indicated by dotted lines in (A). Panza is expressed in the dorsal endoderm of the foregut at the level of the eyes (A1), in the dorsal endoderm adjacent to the notochord in the anterior midgut (A2), and in the dorsal and lateral endoderm of the posterior midgut and hindgut (A3,A4). At the level of the hindgut, Panza expression is also detected in the floorplate of the posterior neural tube (A4). Higher magnification view of a section with the hypochord clearly visible (B). Higher magnification views of Panza and notochord in the posterior end at stage 20 (C), and in the elongating tailbud at stages 33 (D) and 36 (E), showing Panza expression ventral, posterior and dorsal to the notochord. Shown are lateral views of cleared embryos with anterior left (A,C–E) and transverse views with dorsal up (A1–A4,B). de, Dorsal endoderm; e, eyes; fg, foregut; fp, floorplate; h, hypochord; hg, hindgut; mg, midgut; n, notochord; nt, neural tube; s, somite.
	Fig. 4. Panza and Edd expression in the coiled gut and liver. In situ hybridization for Panza (A,A′,C,C′,E,E′,G,G′,I) and Edd (B,D,F,H,J) expression in guts removed from embryos at stages 40 (A,A′,B), 41 (C,C′,D), 42 (E,E′,F), 44 (G,G′,H), and 46 (I,J). Ventral (A,C,E,G) and dorsal (A′,B,C′,D,E′,F,G′,H) views with anterior left are shown. For some samples, the coiled gut was straightened before in situ hybridization and is shown with anterior left (I,J). The brown material apparent in the coiled gut shown in (J) is gut contents present before sample preparation. Arrowheads indicate the position of the liver. gb, Gallbladder; lv, liver; p, pancreas; s, stomach.

References [+] :

Agius, Endodermal Nodal-related signals and mesoderm induction in Xenopus. 2000, Pubmed, Xenbase

Agius, Endodermal Nodal-related signals and mesoderm induction in Xenopus. 2000, Pubmed , Xenbase
Arandjelovic, Growth factor-binding sequence in human alpha2-macroglobulin targets the receptor-binding site in transforming growth factor-beta. 2003, Pubmed
Bergqvist, Hereditary alpha 2-macroglobulin deficiency. 1979, Pubmed
Bolce, Ventral ectoderm of Xenopus forms neural tissue, including hindbrain, in response to activin. 1992, Pubmed , Xenbase
Borth, Binding of IL-1 beta to alpha-macroglobulins and release by thioredoxin. 1990, Pubmed
Borth, Alpha 2-macroglobulin, a multifunctional binding protein with targeting characteristics. 1992, Pubmed
Borth, Identification of alpha 2-macroglobulin as a cytokine binding plasma protein. Binding of interleukin-1 beta to "F" alpha 2-macroglobulin. 1989, Pubmed
Chalmers, Development of the gut in Xenopus laevis. 1998, Pubmed , Xenbase
Cheng, Sertoli cell synthesizes and secretes a protease inhibitor, alpha 2-macroglobulin. 1990, Pubmed
Du, Alpha2-macroglobulin attenuates beta-amyloid peptide 1-40 fibril formation and associated neurotoxicity of cultured fetal rat cortical neurons. 1998, Pubmed
Feige, Alpha 2-macroglobulin: a binding protein for transforming growth factor-beta and various cytokines. 1996, Pubmed
Gaddy-Kurten, Hormonal regulation and tissue-specific localization of alpha 2-macroglobulin in rat ovarian follicles and corpora lutea. 1989, Pubmed
Garber, Interleukin-4 and IL-10 bind covalently to activated human alpha2-macroglobulin by a mechanism that requires Cys949. 2000, Pubmed
Hayashida, Expression of rat alpha 2-macroglobulin gene during pregnancy. 1986, Pubmed
Huang, Specific covalent binding of platelet-derived growth factor to human plasma alpha 2-macroglobulin. 1984, Pubmed
Huang, Human transforming growth factor beta.alpha 2-macroglobulin complex is a latent form of transforming growth factor beta. 1988, Pubmed
Hughes, Alpha2-macroglobulin associates with beta-amyloid peptide and prevents fibril formation. 1998, Pubmed
James, Preliminary studies on the interaction of TNF alpha and IFN gamma with alpha 2-macroglobulin. 1992, Pubmed
Kodelja, Alpha 2-macroglobulin gene expression during rat development studied by in situ hybridization. 1986, Pubmed
Kovacs, alpha2-macroglobulin in late-onset Alzheimer's disease. 2000, Pubmed
Kurdowska, Involvement of alpha-2-macroglobulin receptor in clearance of interleukin 8-alpha-2-macroglobulin complexes by human alveolar macrophages. 2000, Pubmed
Lorent, Distribution of mRNA coding for alpha-2-macroglobulin, the murinoglobulins, the alpha-2-macroglobulin receptor and the alpha-2-macroglobulin receptor associated protein during mouse embryogenesis and in adult tissues. 1994, Pubmed
Mather, Follistatins and alpha 2-macroglobulin are soluble binding proteins for inhibin and activin. 1996, Pubmed
Mathew, Characterization of the interaction between alpha2-macroglobulin and fibroblast growth factor-2: the role of hydrophobic interactions. 2003, Pubmed
Narita, Alpha2-macroglobulin complexes with and mediates the endocytosis of beta-amyloid peptide via cell surface low-density lipoprotein receptor-related protein. 1997, Pubmed
Niemuller, Alpha 2-macroglobulin conformation determines binding affinity for activin A and plasma clearance of activin A/alpha 2-macroglobulin complex. 1995, Pubmed
Northemann, Structure and acute-phase regulation of the rat alpha 2-macroglobulin gene. 1988, Pubmed
Phillips, Regulation of activin's access to the cell: why is mother nature such a control freak? 2000, Pubmed
Ronne, Nerve growth factor binds to serum alpha-2-macroglobulin. 1979, Pubmed
Sasai, Endoderm induction by the organizer-secreted factors chordin and noggin in Xenopus animal caps. 1996, Pubmed , Xenbase
Saunders, Genetic association of Alzheimer's disease with multiple polymorphisms in alpha-2-macroglobulin. 2003, Pubmed
Stouffer, Activated alpha 2-macroglobulin and transforming growth factor-beta 1 induce a synergistic smooth muscle cell proliferative response. 1993, Pubmed
Umans, Targeted inactivation of the mouse alpha 2-macroglobulin gene. 1995, Pubmed
Van Gool, alpha 2-Macroglobulin expression in neuritic-type plaques in patients with Alzheimer's disease. 1993, Pubmed
Wilson, Mesodermal patterning by an inducer gradient depends on secondary cell-cell communication. 1994, Pubmed , Xenbase
Zorn, Gene expression in the embryonic Xenopus liver. 2001, Pubmed , Xenbase