Funisitis is inflammation of the connective tissue of the umbilical cord that occurs with chorioamnionitis. It involves only the external cord surface and Whartons jelly. It has no involvement of the vessels. It does not involve the umbilical stump, which would be seen in omphalitis. Necrotizing funisitis
Necrotizing funisitis is a very severe form of funisitis that occurs when the funisitis has been present for a long time. Debris from inflammatory cells accumulate and the cord becomes calcified. Treatment with IV antibiotics is necessary for necrotizing funisitis, with a minimum of 7 days. This can occur in healthy born infants; the infection occurs in the days and weeks following birth. With IV antibiotic treatment and early management, outcomes are good. Syphilis association
It could be associated with congenital syphilis, which is noted in a journal from 1999. It is now rare, and seen almost exclusively in the preterm infant. The majority of these affected infants are stillborn, or die within a few weeks of birth. See also
Chorioamnionitis
Placentitis


== References ==
C1-inhibitor (C1-inh, C1 esterase inhibitor) is a protease inhibitor belonging to the serpin superfamily. Its main function is the inhibition of the complement system to prevent spontaneous activation but also as the major regulator of the contact system. C1-inhibitor is an acute-phase protein that circulates in blood at levels of around 0.25 g/L. The levels rise ~2-fold during inflammation. C1-inhibitor irreversibly binds to and inactivates C1r and C1s proteases in the C1 complex of classical pathway of complement. MASP-1 and MASP-2 proteases in MBL complexes of the lectin pathway are also inactivated. This way, C1-inhibitor prevents the proteolytic cleavage of later complement components C4 and C2 by C1 and MBL. Although named after its complement inhibitory activity, C1-inhibitor also inhibits proteases of the fibrinolytic, clotting, and kinin pathways. Note that C1-inhibitor is the most important physiological inhibitor of plasma kallikrein, fXIa, and fXIIa. Proteomics
C1-inhibitor is the largest member among the serpin superfamily of proteins. It can be noted that, unlike most family members, C1-inhibitor has a 2-domain structure. The C-terminal serpin domain is similar to other serpins, which is the part of C1-inhibitor that provides the inhibitory activity. The N-terminal domain (also some times referred to as the N-terminal tail) is not essential for C1-inhibitor to inhibit proteases. This domain has no similarity to other proteins. C1-inhibitor is highly glycosylated, bearing both N- and O-glycans. N-terminal domain is especially heavily glycosylated. Genetics
The human C1-inhibitor gene (SERPING1) is located on the eleventh chromosome (11q11-q13.1).