Purification and characterization of CRISP-3 from human seminal plasma and its real-time binding kinetics with PSP94

Anklesaria, Jenifer H.; Pandya, Rushika R.; Pathak, Bhakti R.; Mahale, Smita D.

doi:10.1016/j.jchromb.2016.10.032

Cited by 10 publications

(9 citation statements)

References 24 publications

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“…Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI TOF MS) is a powerful analytical technique widely used for analysis of proteins in a broad range of biological samples which vary from lysed cells extracts [1][2][3][4][5][6][7][8][9][10] to tissue sections [11][12][13][14][15][16][17][18]. Whole cell MALDI fingerprinting is based on the mass spectral analysis of a whole cell without additional preparatory steps such as fractionation or extraction.…”

Section: Introductionmentioning

confidence: 99%

Whole Cell MALDI Fingerprinting Is a Robust Tool for Differential Profiling of Two-Component Mammalian Cell Mixtures

Petukhova

Young

Wang³

et al. 2018

J. Am. Soc. Mass Spectrom.

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MALDI fingerprinting was first described two decades ago as a technique to identify microbial cell lines. Microbial fingerprinting has since evolved into an automated platform for microorganism identification and classification which is now routinely used in clinical and environmental sectors. The extension of fingerprinting to mammalian cells has yet to progress partly due to compartmentalization of eukaryotic cells and overall higher cellular complexity. A number of publications on mammalian whole cell fingerprinting suggests that the method could be useful for classification of different cell types, cell states, and monitoring cell differentiation. We report the optimization of MALDI fingerprinting workflow parameters for mammalian cells and its application for differential profiling of mammalian cell lines and two component cell line mixtures. Murine fallopian tube cells and high-grade ovarian carcinoma cell lines and their mixtures are used as model mammalian cell lines. Two-component cell mixtures serve to determine the method's feasibility for complex biological samples as the ability to detect cancer cells in a mixed cell population. The level of detection of cancer cells in the two-component mixture by principle component analysis (PCA) starts to deteriorate at 5% but with application of a different statistical approach, Wilcoxon rank sum test, the level of detection was determined to be 1%. The ability to differentiate heterogeneous cell mixtures will help further extend whole cell MALDI fingerprinting to complex biological systems.

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Section: Introductionmentioning

confidence: 99%

Whole Cell MALDI Fingerprinting Is a Robust Tool for Differential Profiling of Two-Component Mammalian Cell Mixtures

Petukhova

Young

Wang³

et al. 2018

J. Am. Soc. Mass Spectrom.

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“…innate immunity has been proposed [10]. Additionally, it has been shown that CRISP-3 forms complexes with α1B-glycoprotein in blood plasma [11] and PSP94 in seminal plasma [12,13]. More recently, CRISPs were identified in the venom of several animals, presenting different functions.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

“…However, future studies are needed to precisely determine the stoichiometric arrangement of these oligomeric forms. On the other hand, some reports have shown that CRISP-3 from human plasma can form complexes with human blood plasma proteins (α1B-glycoprotein-A1BG) [11] and seminal proteins (prostate secretory protein of 94 amino acids-PSP94) [12,13]. In these cases, the proteins complexed with CRISP-3 would act as protectors of the harmful effects of free CRISP-3.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Biochemical and structural characterization of a protein complex containing a hyaluronidase and a CRISP-like protein isolated from the venom of the spider Acanthoscurria natalensis

Barth

Mandacaru

Charneau

et al. 2019

Journal of Proteomics

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“…A metal-ion-binding site in the CAP/PR-1 domain of CRISPs is also well conserved (His60, Glu75, Glu96, and His115; triflin numbering). Human CRISPs contain a glycosylation site (Asn-X(except Pro)-Ser/Thr) and a glycosylated form exists [43], but very few svCRISPs share this feature [41]. Amino-acid sequence alignments of Cysteine-rich secretory proteins (CRISPs).…”

Section: Cap/pr-1 Domainmentioning

confidence: 99%

“…As previously discussed, the CRD/ICR domain is one of the CRISP regions potentially responsible for targeting ion-channels. This has been suggested because this domain is very similar to peptides that block ion channels, including peptide toxins KTX, α-KTX, and ShTx (43). CRD/ICR domain sequences between CRISPs that cause muscle contraction and those that inhibit contractions were compared ( Figure 3A).…”

Section: Potential Domains and Functional Sites Responsible For Ion Cmentioning

confidence: 99%

Cysteine-Rich Secretory Proteins (CRISPs) from Venomous Snakes: An Overview of the Functional Diversity in a Large and Underappreciated Superfamily

Tadokoro

Modahl

Maenaka

et al. 2020

Toxins

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The CAP protein superfamily (Cysteine-rich secretory proteins (CRISPs), Antigen 5 (Ag5), and Pathogenesis-related 1 (PR-1) proteins) is widely distributed, but for toxinologists, snake venom CRISPs are the most familiar members. Although CRISPs are found in the majority of venoms, very few of these proteins have been functionally characterized, but those that have been exhibit diverse activities. Snake venom CRISPs (svCRISPs) inhibit ion channels and the growth of new blood vessels (angiogenesis). They also increase vascular permeability and promote inflammatory responses (leukocyte and neutrophil infiltration). Interestingly, CRISPs in lamprey buccal gland secretions also manifest some of these activities, suggesting an evolutionarily conserved function. As we strive to better understand the functions that CRISPs serve in venoms, it is worth considering the broad range of CRISP physiological activities throughout the animal kingdom. In this review, we summarize those activities, known crystal structures and sequence alignments, and we discuss predicted functional sites. CRISPs may not be lethal or major components of venoms, but given their almost ubiquitous occurrence in venoms and the accelerated evolution of svCRISP genes, these venom proteins are likely to have functions worth investigating.

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Purification and characterization of CRISP-3 from human seminal plasma and its real-time binding kinetics with PSP94

Cited by 10 publications

References 24 publications

Whole Cell MALDI Fingerprinting Is a Robust Tool for Differential Profiling of Two-Component Mammalian Cell Mixtures

Whole Cell MALDI Fingerprinting Is a Robust Tool for Differential Profiling of Two-Component Mammalian Cell Mixtures

Biochemical and structural characterization of a protein complex containing a hyaluronidase and a CRISP-like protein isolated from the venom of the spider Acanthoscurria natalensis

Cysteine-Rich Secretory Proteins (CRISPs) from Venomous Snakes: An Overview of the Functional Diversity in a Large and Underappreciated Superfamily

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