Spasmin-like proteins in various ciliates revealed by antibody to purified spasmins ofCarchesium polypinum

Abstract

It was found that some ciliates, Stentor, Spirostomum and Blepharisma, which can contract rapidly like the stalks of Vorticellidae, have Ca2+-binding proteins that are very similar to spasmins, in the immunological sense. The presence of spasmins in other Protozoa and in some Metazoa was also investigated.

Identification and Localization of a Protein Immunologically Related to Caltractin (Centrin) in the Myonemes and Membranelles of the Heterotrich Ciliate Stentor coeruleus

“…Spasmin, like caltractin, is an acidic protein with an MW of 20 kDa that has an altered electrophoretic mobility in the presence of Ca 21 , but it appears to be a different protein (Maciejewski et al 1999). Ochiai et al (1988) used an antibody to spasmin isolated from Carchesium polypinum to identify three to four related proteins between 15 and 20 kDa in Stentor, Blepharisma, and Spirostomum, substantiating the idea that spasmin is present in these contractile ciliates. However, no protein in the MW range of 23 kDa was recognized by this anti-spasmin antibody.…”

“…The protein composition of the myonemes of Stentor is unknown, although it has been assumed that the major component is likely to be spasmin, based on similarities in the structure and properties of the spasmoneme and the myonemes. Ochiai et al (1988) prepared an antibody to spasmin from Carchesium and showed by protein blotting that this antibody recognized four proteins in Stentor that range in molecular weight (MW) from 15 to 20 kDa, indicating that proteins immunologically related to spasmin are present in Stentor . Whether these proteins are located in the myonemes was not shown, as no immunofluorescence studies were performed.…”

Centrin inGiardia lamblia– ultrastructural localization

“…Ochiai et al [14] described a 20 kDa spasmin‐like protein in several protists, including ciliates and flagellates. These authors isolated contractile stalks and demonstrated that contraction of these structures was due to the presence of Ca 2+ ‐binding proteins.…”

Vorticella: A Protozoan for Bio-Inspired Engineering

“…This difference is due to a structural difference of the spasmoneme between the two species: the Zoothamnium spasmoneme is continuous among zooids in the colony, whereas the Carchesium spasmoneme is discontinuous between zooids. Because Zoothamnium and Carchesium have bigger spasmonemes than Vorticella does (the spasmoneme of Zoothamnium is about 30 μm in diameter and 1 mm long [ 30 ]), they have also been employed for studying the spasmonemal contraction [ 10 , 30 , 31 , 32 , 33 , 34 , 35 , 36 , 37 , 38 , 39 , 40 , 41 , 42 , 43 , 44 , 45 , 46 , 47 , 48 , 49 , 50 , 51 , 52 , 53 , 54 , 55 , 56 , 57 ].…”