Avian thymic hormone (ATH) is a parvalbumin

Brewer, John M.; Wunderlich, John K.; Kim, Dooha; Carr, Michel Y.; Beach, G.G.; Ragland, W.L.

doi:10.1016/s0006-291x(89)80124-x

Cited by 41 publications

(17 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The appearance of PV-like positivity on day 9 coincides in time with the invasion of the lymphoid elements in the cordlike gland and the beginning of their maturation (Romanoff 1960). These phenomena have been considered to be under the control of a secreted hormone (ATH) that is similar in sequence to PV (Brewer et al 1989;Henzl 1990, 1991a, b;Henzl et al 1991 ;Serda and Henzl 1991). In the classical experiments of Ragland and co-workers (Barger et al 1977;Murthy and Ragland 1984;Murthy et al 1984a, b) a thymus extract was added to the thymocytes to demonstrate the presence of the promoting factor (ATH) in vitro.…”

Section: Calretinin Discussionmentioning

confidence: 99%

“…For more than a decade Ragland and his coworkers (Barger et al 1977;Murthy and Ragland 1984) have studied a protein isolated from chicken thymus, called Avian Thymic Hormone (ATH), and have found that it promotes the development of T-lymphocytes (Murthy et al 1984a, b). It has been reported that the nucleic acid sequence of ATH (Brewer et al 1989;Henzl 1990, 1991a, b;Henzl et al 1991 ;Serda and Henzl 1991) is nearly the same as that of parvalbumin (PV) from chicken, turtle and amphibian muscle (Strehler et al 1977;Heizmann and Strehler 1979;Hall et al 1991). Since PV is found intracellularly in muscles (P6ch~re et al 1973;Celio and Heizmann 1982) and brain (Celio and Correspondence to: M.R.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Parvalbumin and calretinin in the avian thymus

Király

Celio

1993

Anat Embryol

View full text Add to dashboard Cite

The avian thymic hormone, known to support the maturation of T-lymphocytes, is biochemically similar to parvalbumin. However, its exact cellular distribution in the thymus is unknown. We have therefore studied the occurrence of parvalbumin and other related calcium-binding proteins in this organ by immunohistochemistry during development and after hatching. Parvalbumin immunoreactivity appears in the epithelial cells on embryonic day 9, and is expressed in the cortical reticular cells in the adult. Calretinin is found in the clusters of medullary epithelial cells from embryonic day 11, whereas calbindin D-28k is absent from this organ. Thus, calcium binding-proteins are excellent markers for different compartments of the avian thymus in embryonic life and after hatching, and their expression seems to coincide with their functional maturation.

show abstract

Section: Calretinin Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Parvalbumin and calretinin in the avian thymus

Király

Celio

1993

Anat Embryol

View full text Add to dashboard Cite

show abstract

“…Thus, the role of OM as a putative neurotrophic factor is a novel exciting topic, but it is certainly too early to make any conclusive statements. An action as a hormone, i.e., to promote immunological maturity in chicken bone marrow cells in culture, was also reported for the second b lineage type PV, called avian thymic hormone (ATH) [93]. ATH has also two Ca 2+ /Mg 2+ mixed sites similar to the "muscle and neuron"-type PV [94] and unlike OM that contains a Ca 2+ -specific and a mixed Ca 2+ /Mg 2+ site.…”

mentioning

confidence: 97%

The continuing disappearance of “pure” Ca2+ buffers

Schwaller

2008

Cell. Mol. Life Sci.

226

201

View full text Add to dashboard Cite

Advances in the understanding of a class of Ca(2+)-binding proteins usually referred to as "Ca(2+) buffers" are reported. Proteins historically embraced within this group include parvalbumins (alpha and beta), calbindin-D9k, calbindin-D28k and calretinin. Within the last few years a wealth of data has accumulated that allow a better understanding of the functions of particular family members of the >240 identified EF-hand Ca(2+)-binding proteins encoded by the human genome. Studies often involving transgenic animal models have revealed that they exert their specific functions within an intricate network consisting of many proteins and cellular mechanisms involved in Ca(2+) signaling and Ca(2+) homeostasis, and are thus an essential part of the Ca(2+) homeostasome. Recent results indicate that calbindin-D28k, possibly also calretinin and oncomodulin, the mammalian beta parvalbumin, might have additional Ca(2+) sensor functions, leaving parvalbumin and calbindin-D9k as the only "pure" Ca(2+) buffers.

show abstract

“…p parvalbumins might have different functions. The discovery of an avian thymic hormone (ATH) in chicken, which is a p parvalbumin promoting lymphocyte maturation and circulating in the blood stream, suggests extracellular and hormone-like functions (Brewer et a]., 1989;Brewer et al, 1990). However, in contrast to the chicken p parvalbumin (ATH) the roles of / 3 parvalbumins in other species are still unknown.…”

Section: Expression Of a And P Parvalbumins In Human Tissuesmentioning

confidence: 99%

Human α and β parvalbumins

Föhr

Weber

Müntener

et al. 1993

European Journal of Biochemistry

View full text Add to dashboard Cite

α and β parvalbumins are Ca2+‐binding proteins of the EF‐hand type. We determined the protein sequence of human brain α parvalbumin by mass spectrometry and cloned human β parvalbumin (or oncomodulin) from genomic DNA and preterm placental cDNA. β parvalbumin differs in 54 positions from α parvalbumin and lacks the C‐terminal amino acid 109. From MS analyses of α and β parvalbumins we conclude that parvalbumins generally lack posttranslational modifications. α and β parvalbumins were differently expressed in human tissues when analyzed by immunoblotting and polymerase‐chain‐reaction techniques. Whereas α parvalbumin was found in a number of adult human tissues, β parvalbumin was restricted to preterm placenta. The pattern of α parvalbumin expression also differs in man compared to other vertebrates. For example, in rat, α parvalbumin was found in extrafusal and intrafusal skeletal‐muscle fibres whereas, in man, α parvalbumin was restricted to the muscle spindles. Different functions for α and β parvalbumins are discussed.

show abstract

Avian thymic hormone (ATH) is a parvalbumin

Cited by 41 publications

References 6 publications

Parvalbumin and calretinin in the avian thymus

Parvalbumin and calretinin in the avian thymus

The continuing disappearance of “pure” Ca2+ buffers

Human α and β parvalbumins

Contact Info

Product

Resources

About