Role of Matrix Metalloproteases and Total Antioxidant Capacity in Early Childhood Caries – A Review | Chapter 10 | Advanced Concepts in Medicine and Medical Research Vol. 12

Dentistry has traditionally transitioned from the straightforward extraction of the caries-affected tooth to the treatment and restoration of the lesion in the evolution of caries therapy. A further development in dental care is the detection of early caries lesions and treatment using non-surgical techniques like remineralization. The phrases early childhood caries and rampant caries are occasionally used interchangeably. More than 25 secreted and membrane-bound enzymes collectively referred to as matrix metalloproteinases are a class of enzymes that break down pericellular substrates. The amount of free radicals scavenged by a test solution is measured as the total antioxidant capacity, which is then used to assess the antioxidant strength of biological samples. This is very important because oxidative stress can influence the beginning and development of various nflammatory and infectious disorders, including dental caries. The purpose of this review is to talk about how total antioxidant capacity and matrix metalloproteases relate to early childhood caries.

Author(s) Details:

Umapathy Thimmegowa,
Department of Pediatric and Preventive Dentistry, Raja Rajeswari Dental College and Hospital, No 14, Ramohalli Cross, Kumbalgodu, Mysore Road, Bengaluru-560074, India.

Soumya Pai,
Department of Pediatric and Preventive Dentistry, Raja Rajeswari Dental College and Hospital, No 14, Ramohalli Cross, Kumbalgodu, Mysore Road, Bengaluru-560074, India.

Praveen Malavalli Nagarajshetty,
Department of Orthodontics and Dentofacial Orthopaedics, KLE’ S Institute of Dental Sciences, Yeshwanthpur Suburb, Tumkur Road, Bengaluru- 560022, India.

Please see the link here: https://stm.bookpi.org/ACMMR-V12/article/view/12996

The Role of Actin-specific Bacterial Endoproteases Grimelysin and Protelysin in Serratia Invasion | Chapter 11 | Research Advances in Microbiology and Biotechnology Vol. 8

 This branch describes the features of the bacterial proteases grimelysin and protealysin, which are resentment factors in vitro and in vivo, and actin maybe a target for these proteases upon their fluctuation into the host cell.Bacterial encroachment into eukaryotic cells is individual of the major areas of research in contamination biology, by which they employ various strategies to ravage the host cells. These interactions are very complex, and the type of interaction depends on the germ, host, as well as tangible factors. The alone actin polypeptide link, Gly42-Val43, is broken by grimelysin. No other proteases are capable to break this link, which results in the erratic loss of actin polymerization. Similar traits were shared by protealysin, another bacterial protease. Grimelysin and protealysin are singular tools for studying the working characteristics of actin by way of their characteristics. Furthermore, microorganisms Serratia grimesii and Serratia proteamaculans, producing grimelysin and protealysin, infest eukaryotic cells, and the recombinant Escherichia coli expressing the grimelysin or protealysins deoxyribonucleic acid become obtrusive. Specifically, the grimelysin (ECP 32)-producing microorganisms invaded the altered epithelial and fibroblasts cells A431, HeLa and 3T3-SV40, but they were not about embryonic fibroblasts, primary human keratinocytes and in containers of poorly transformed 3T3 container lines. The invasion of eukaryotic containers by S. grimesii has been explained to include the cellular c-Src and RhoA/ROCK indicating pathways, and it has also happened proposed that E-cadherin plays a duty in the invasion. Furthermore, it was found that S. grimesii produces membrane vesicles that contain grimelysin, introduce eukaryotic cells, and advance bacterial invasion of these containers. These data signify that the protease is a virulence factor, and actin maybe a target for the protease upon allure translocation into the host container.

Author(s) Details:

Sofia Khaitlina,
Institute of Cytology, Russian Academy of Sciences, 194064 St. Petersburg, Russia.

Ekaterina Bozhokina,
Institute of Cytology, Russian Academy of Sciences, 194064 St. Petersburg, Russia.

Olga Tsaplina,
Institute of Cytology, Russian Academy of Sciences, 194064 St. Petersburg, Russia.

Tatiana Efremova,
Institute of Cytology, Russian Academy of Sciences, 194064 St. Petersburg, Russia.

Please see the link here: https://stm.bookpi.org/RAMB-V8/article/view/12631